column_label: Table 3; row substrate 1 alpha-phenylalanine / L-Phenylalanine; enzyme TcPAM (wild_type); columns K_M (M)x10^3, beta-kcat (s^-1), beta-kcat/K_M (M^-1 s^-1); cells 0.057 (+/-0.004), 0.053 (+/-0.01), 930 (+/-20).

normalized_value_unit_evidence: K_M 0.057 mM; beta-kcat 0.053 s^-1; beta-kcat/K_M 930 M^-1 s^-1 = 0.93 s^-1*mM^-1; exported kcat/K_M 0.929825 is consistent with beta-kcat/K_M after table rounding or kcat/K_M recomputation from beta-kcat and K_M.

raw_value_unit_evidence: Table 3 row substrate 1 alpha-phenylalanine / L-Phenylalanine; enzyme TcPAM (wild_type): K_M 0.057 (+/-0.004) mM; beta-kcat 0.053 (+/-0.01) s^-1; beta-kcat/K_M 930 (+/-20) M^-1 s^-1. Sibling columns: cin-kcat 0.012 (+/-0.002) s^-1; total kcat/K_M 1100 (+/-100) M^-1 s^-1.


organism: Dirofilaria immitis

source_db: oed

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

source: oed


enzyme_display_name: isochorismate synthase

organism: Arabidopsis thaliana

substrate_name: Chorismate

verification_status: unverified

enzyme: isochorismate synthase

substrate: Chorismate

status: unverified


substrate_name: magnesium

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

smiles: [Mg]

substrate: magnesium

source: uniprot


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: isochorismate

assay_conditions_summary: pH 8

proof_lines: kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-1) for isochorismate synthase activity (

substrate: isochorismate


substrate_name: chorismate

substrate: chorismate


organism: Caenorhabditis elegans

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

sequence_source: multiple

source_databases_merged: sabio_rk brenda uniprot


enzyme_display_name: glutamate 2,3-aminomutase

organism: Clostridioides difficile (strain 630)

substrate_name: L-glutamate

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

proof_lines: kcat is 6.1 sec(-1) with L-glutamate as substrate.

enzyme: glutamate 2,3-aminomutase

substrate: L-glutamate


organism: Trypanosoma brucei


enzyme_display_name: (hydroxyamino)benzene mutase

organism: Ectopseudomonas oleovorans

substrate_name: hydroxylaminobenzene (at pH 7)

enzyme: (hydroxyamino)benzene mutase

substrate: hydroxylaminobenzene (at pH 7)


organism: Bacillus subtilis

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


organism: Pyrococcus furiosus

source_db: brenda

verification_status: verified

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

assay_conditions_summary: pH 8; buffer 200 mM Tris-maleate

column_label: Table 1 lists PF1959 Km 3-phosphoglycerate (mM) = 0.49 +/- 0.06.

raw_value_unit_evidence: Km raw_value=0.49 +/- 0.06 mM raw_unit=mM

row_label: Km 3-phosphoglycerate (mM), PF1959 / P. furiosus column

table_label: Oxford Academic Table 1: The iPGMs of the archaea P. furiosus and M. jannaschii

status: verified

source: brenda


organism: Onchocerca volvulus


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A213K to reconstruct the assayed variant sequence.

mutation_type: substitution


enzyme_display_name: phenylalanine aminomutase (L-beta-phenylalanine forming)

organism: Taxus chinensis

substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor NADPH

column_label: Table 2; reaction GPM; isoenzyme Gpm1p; parameter kcat value 400 s^-1; parameter Kp2g value 1.41 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=400 normalized_unit=s^-1; Km normalized_value=1.41 normalized_unit=mM; kcat/Km normalized_value=283.68794326241135 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=400 raw_unit=s^-1; Km raw_value=1.41 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 400/1.41 raw_unit=s^-1*mM^-1

row_label: GPM / Gpm1p / Kp2g

table_label: Table 2. Enzyme kinetics parameters determined in this project and contrasted with those of [23].


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH


enzyme_display_name: tyrosine 2,3-aminomutase

organism: Streptomyces globisporus

substrate_name: L-Tyrosine

proof_lines: pH and temperature not specified in the publication

enzyme: tyrosine 2,3-aminomutase

substrate: L-Tyrosine


substrate_name: D-alpha-phenylalanine

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

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

enzyme: phenylalanine aminomutase (L-beta-phenylalanine forming)

substrate: D-alpha-phenylalanine


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


proof_lines: pH and temperature not specified in the publication, recombinant mutant L97G/C89T


substrate_name: L-beta-phenylalanine

substrate: L-beta-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


proof_lines: pH and temperature not specified in the publication, recombinant mutant L97G


substrate_name: L-beta-tyrosine

substrate: L-beta-tyrosine


organism: Mus musculus


enzyme_display_name: D-ornithine 4,5-aminomutase

organism: Acetoanaerobium sticklandii

substrate_name: D-ornithine

km_display: Not reported

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

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E81D

enzyme: D-ornithine 4,5-aminomutase

substrate: D-ornithine


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E81A


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E81Q


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant R297K


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant N226D


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


assay_conditions_summary: pH 7

proof_lines: mutant enzyme F327Y/I346L, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme A303T, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F327Y, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F359Q/I346L, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F327Y/F359Q, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme I346L, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F359Q, in 100 mM phosphate pH 7.0, 10 mM MgCl2


organism: Pseudomonas aeruginosa


organism: Cupriavidus metallidurans


organism: Chondromyces crocatus


enzyme_display_name: pancreatic ribonuclease

organism: Bos taurus

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

enzyme: pancreatic ribonuclease

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


enzyme_display_name: methylmalonyl-CoA mutase

organism: Ovis aries

substrate_name: succinyl-CoA

enzyme: methylmalonyl-CoA mutase

substrate: succinyl-CoA


substrate_name: L-Dopa

substrate: L-Dopa


enzyme_display_name: protein disulfide-isomerase

substrate_name: ribonuclease

proof_lines: dithiothreitol, with scrambled ribonuclease as substrate

proof_lines: scrambled, with dithiothreitol as substrate

enzyme: protein disulfide-isomerase

substrate: ribonuclease


smiles: C(CS)O

proof_lines: with scrambled ribonuclease as substrate


substrate_name: cysteine

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

proof_lines: GSH, with scrambled ribonuclease as substrate

substrate: cysteine


enzyme_display_name: thromboxane-A synthase

organism: Homo sapiens

substrate_name: prostaglandin H3

enzyme: thromboxane-A synthase

substrate: prostaglandin H3


substrate_name: prostaglandin G2

substrate: prostaglandin G2


substrate_name: Prostaglandin H1

substrate: Prostaglandin H1


proof_lines: recombinant His-tagged mutant E338D, pH 7.5, 30°C

proof_lines: recombinant beta-subunit mutant E338D, pH 8.5, 25°C


proof_lines: recombinant His-tagged wild-type enzyme, pH 7.5, 30°C

proof_lines: pH 8.5, 20°C, recombinant wild-type enzyme


proof_lines: recombinant His-tagged mutant E338Q, pH 7.5, 30°C

proof_lines: recombinant beta-subunit mutant E338Q, pH 8.5, 25°C


sequence_source: UniProtKB E3PY95

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant P343W


sequence_variant_note: Mutation signature E338A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E338A

proof_lines: recombinant His-tagged mutant E338A, pH 7.5, 30°C

proof_lines: recombinant beta-subunit mutant E338A, pH 8.5, 25°C


sequence_variant_note: Mutation signature I424E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant I424E


sequence_variant_note: Mutation signature D627A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant D627A


enzyme_display_name: protoporphyrin ferrochelatase

organism: Rattus norvegicus

substrate_name: mesoporphyrin IX

enzyme: protoporphyrin ferrochelatase

substrate: mesoporphyrin IX


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


organism: Propionibacterium freudenreichii subsp. shermanii

assay_conditions_summary: cofactor CoA


organism: Colletotrichum gloeosporioides

substrate_name: palmitoleate

smiles: CCCCCCC=CCCCCCCCC(=O)[O-]

proof_lines: recombinant enzyme, whole enzyme activity, pH 6.5, 40°C

substrate: palmitoleate


substrate_name: oleate

smiles: CCCCCCCCC=CCCCCCCCC(=O)[O-]

substrate: oleate


substrate_name: alpha-linolenate

smiles: CCC=CCC=CCC=CCCCCCCCC(=O)[O-]

substrate: alpha-linolenate


smiles: CCCCCC=CCC=CC(CCCCCCC(=O)O)OO


enzyme_display_name: methylaspartate mutase

organism: Clostridium tetanomorphum

substrate_name: adenosylcobalamin

proof_lines: kcat is 20.6 sec(-1) for mutase activity with L-glutamate.

enzyme: methylaspartate mutase

substrate: adenosylcobalamin


substrate_name: L-glutamate

substrate: L-glutamate


organism: Streptomyces ansochromogenes

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


organism: Mammalia


substrate_name: methylmalonyl-carba(dethia)-coenzyme A

substrate: methylmalonyl-carba(dethia)-coenzyme A


organism: Escherichia coli

substrate_name: Chorismate

substrate: Chorismate


sequence_variant_note: Mutation signature H610A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: 310.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H610A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H610N to reconstruct the assayed variant sequence.


substrate_name: methylmalonyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y89F to reconstruct the assayed variant sequence.

substrate: methylmalonyl-CoA


enzyme_display_name: 3-(hydroxyamino)phenol mutase

organism: Cupriavidus necator

proof_lines: The values are approximate data due to the instability of the substrate.

source_databases_merged: brenda uniprot

enzyme: 3-(hydroxyamino)phenol mutase


enzyme_display_name: geraniol isomerase

organism: Castellaniella defragrans

substrate_name: geraniol

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

assay_conditions_summary: pH 9

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

enzyme: geraniol isomerase

substrate: geraniol


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


substrate_name: Unknown

substrate: Unknown


organism: Caenorhabditis elegans

proof_lines: with apo-enzyme, pH 7.0, temperature not specified in the publication


organism: Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)


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


organism: Emericella nidulans


organism: Gaeumannomyces graminis


enzyme_display_name: hydroperoxy icosatetraenoate isomerase

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

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

enzyme: hydroperoxy icosatetraenoate isomerase


enzyme_display_name: linalool isomerase

organism: Thauera linaloolentis (strain DSM 12138 / JCM 21573 / CCUG 41526 / CIP 105981 / IAM 15112 / NBRC 102519 / 47Lol)

enzyme: linalool isomerase


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


sequence_variant_note: Mutation signature Y89A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y89F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Clostridium cochlearium

substrate_name: L-Glutamate

substrate: L-Glutamate


substrate_name: Coenzyme B12

substrate: Coenzyme B12


organism: Taxus canadensis

substrate_name: styryl-alpha-alanine

substrate: styryl-alpha-alanine


substrate_name: L-phenylalanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L104A to reconstruct the assayed variant sequence.

substrate: L-phenylalanine


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


smiles: CC/C=C\C/C=C\C/C=C\CCCCCCCC(=O)O


smiles: CCCCCCCC/C=C\CCCCCCCC(=O)O


smiles: CCCCCC/C=C\CCCCCCCC(=O)O


substrate_name: palmitoleic acid

smiles: CCCCCCC=CCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 16:1delta9Z; column Km = 5.00 +/- 0.85 umol/liter

raw_value_unit_evidence: Table 3 row 16:1delta9Z (palmitoleic acid); Km = 5.00 +/- 0.85 umol/liter

substrate: palmitoleic acid


substrate_name: oleic acid

smiles: CCCCCCCC=CCCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 18:1delta9Z; column Km = 6.71 +/- 0.74 umol/liter

raw_value_unit_evidence: Table 3 row 18:1delta9Z (oleic acid); Km = 6.71 +/- 0.74 umol/liter

substrate: oleic acid


substrate_name: linoleic acid

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

column_label: Table 3. Kinetic parameters for different substrates; row 18:2delta9Z,12Z; column Km = 18.30 +/- 2.6 umol/liter

raw_value_unit_evidence: Table 3 row 18:2delta9Z,12Z (linoleic acid); Km = 18.30 +/- 2.6 umol/liter

substrate: linoleic acid


substrate_name: alpha-linolenic acid

smiles: CCC=CCC=CCC=CCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 18:3delta9Z,12Z,15Z; column Km = 22.6 +/- 4.3 umol/liter

raw_value_unit_evidence: Table 3 row 18:3delta9Z,12Z,15Z (alpha-linolenic acid); Km = 22.6 +/- 4.3 umol/liter

substrate: alpha-linolenic acid


substrate_name: oxygen

smiles: O=O

column_label: Abstract reports Km values were 8 microM for linoleic acid and 30 microM for oxygen.

raw_value_unit_evidence: Km raw_value=30 microM raw_unit=microM

row_label: Gaeumannomyces graminis linoleate 8-dioxygenase / oxygen

table_label: PubMed XML abstract PMID 8662736

substrate: oxygen


raw_value_unit_evidence: Km raw_value=8 microM raw_unit=microM

row_label: Gaeumannomyces graminis linoleate 8-dioxygenase / linoleic acid


organism: Homo sapiens

substrate_name: adenosylcob(III)alamin

substrate: adenosylcob(III)alamin


substrate_name: L-glutamate

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


proof_lines:
23°C, wild-type enzyme
25°C, wild-type enzyme


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

assay_conditions_summary: pH 8.5; 298.15 K; cofactor CoA

source_databases_merged: sabio_rk skid uniprot


organism: Mus musculus


substrate_name: (R)-methylmalonyl-CoA

proof_lines: recombinant His-tagged mutant E392D, pH 8.5, 25°C

substrate: (R)-methylmalonyl-CoA


proof_lines: recombinant His-tagged mutant E392Q, pH 8.5, 25°C


proof_lines: recombinant His-tagged mutant E392A, pH 8.5, 25°C


proof_lines: recombinant His-tagged wild-type enzyme, pH 8.5, 25°C


organism: Rhizobium meliloti (strain 1021)

substrate_name: (R,S)-methylmalonyl-CoA (in the presence of 3 mM NH4(+))


organism: Propionibacterium freudenreichii subsp. shermanii

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA


substrate_name: Ethylmalonyl-CoA

substrate: Ethylmalonyl-CoA


organism: Euglena gracilis

assay_conditions_summary: pH 7.5; buffer 100 mM potassium phosphate; cofactor CoA

column_label: Results prose reports apparent Km values of 55.8 uM for (R,S)-methylmalonyl-CoA, 27.9 uM for R-methylmalonyl-CoA, and 347.4 uM for succinyl-CoA in the reverse reaction.

raw_value_unit_evidence: Km raw_value=27.9 raw_unit=uM

row_label: Euglena methylmalonyl-CoA mutase forward reaction

table_label: Springer/PDF Results prose - Some properties of Euglena MCM


substrate_name: succinyl-CoA

raw_value_unit_evidence: Km raw_value=347.4 raw_unit=uM

row_label: Euglena methylmalonyl-CoA mutase reverse reaction

substrate: succinyl-CoA


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-cystathionine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystathionine


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: L-cystine

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

substrate: L-cystine


enzyme_display_name: L-3-cyanoalanine synthase

organism: Spinacia oleracea

enzyme: L-3-cyanoalanine synthase


substrate_name: chloroalanine

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

proof_lines:
vs. L-cysteine
26°C, pH 9.8

substrate: chloroalanine


substrate_name: Unknown

proof_lines:
vs. O-acetyl-L-serine
vs. chloroalanine
vs. L-cysteine

substrate: Unknown


organism: Thauera linaloolentis

substrate_name: geraniol

column_label: Abstract reports a specific activity of 3.42+/-0.28 nkat mg protein(-1) and a kM value of 455+/-124 microM for the thermodynamically favored isomerization of geraniol to both linalool isomers at pH 8 and 35 C.

raw_value_unit_evidence: Km raw_value=455+/-124 microM raw_unit=microM

row_label: Thauera linaloolentis 47Lol linalool isomerase / geraniol

table_label: PubMed XML abstract PMID 26979141

substrate: geraniol


assay_conditions_summary: 298.15 K; cofactor CoA


substrate_name: beta-myrcene

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

substrate: beta-myrcene


organism: Sus scrofa

substrate_name: hemin

substrate: hemin


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


substrate_name: protoporphyrin

substrate: protoporphyrin


substrate_name: mesoporphyrin

substrate: mesoporphyrin


proof_lines:
cosubstrate protoporphyrin
cosubstrate mesoporphyrin


substrate: L-glutamate


enzyme_display_name: UniProt A9S498

organism: Physcomitrium patens

substrate_name: chorismate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A9S498

substrate: chorismate

source: skid


enzyme_display_name: UniProt P39912

organism: Bacillus subtilis

enzyme: UniProt P39912


enzyme_display_name: UniProt Q48485

organism: Klebsiella pneumoniae

substrate_name: UDP-D-galactopyranose

enzyme: UniProt Q48485

substrate: UDP-D-galactopyranose


enzyme_display_name: UniProt Q4W1X2

organism: Aspergillus fumigatus

substrate_name: UDP-beta-L-arabinofuranose

enzyme: UniProt Q4W1X2

substrate: UDP-beta-L-arabinofuranose


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


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


enzyme_display_name: lactoylglutathione lyase

organism: Trypanosoma cruzi

substrate_name: glutathionylspermidine

proof_lines:
with phenylglyoxal
with methylglyoxal

enzyme: lactoylglutathione lyase

substrate: glutathionylspermidine


substrate_name: trypanothione

proof_lines: pH and temperature not specified in the publication

substrate: trypanothione


substrate_name: glutathione

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

proof_lines:
with methylglyoxal
with phenylglyoxal

substrate: glutathione


enzyme_display_name: phosphoacetylglucosamine mutase

organism: Aedes aegypti

enzyme: phosphoacetylglucosamine mutase


enzyme_display_name: methionine gamma-lyase

organism: Streptomyces avermitilis

enzyme: methionine gamma-lyase

substrate: L-cysteine


substrate_name: L-homocysteine

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

substrate: L-homocysteine


substrate_name: L-methionine

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

substrate: L-methionine


organism: Aspergillus niger


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


enzyme_display_name: methylmalonyl-CoA mutase

organism: Homo sapiens

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

enzyme: methylmalonyl-CoA mutase


enzyme_display_name: chorismate mutase

organism: Kitasatospora aureofaciens

enzyme: chorismate mutase


enzyme_display_name: 2-acetolactate mutase

organism: Mycobacterium tuberculosis

enzyme: 2-acetolactate mutase


enzyme_display_name: lanosterol synthase

enzyme: lanosterol synthase


organism: Ustilago maydis

substrate_name: Chorismate

substrate: Chorismate


substrate_name: Unknown

substrate: Unknown


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: succinyl-CoA

proof_lines: kcat is 48 sec(-1) with succinyl-CoA as substrate.

substrate: succinyl-CoA


organism: Ruta graveolens

proof_lines:
enzyme form CM2
enzyme CM1


enzyme_display_name: cycloartenol synthase

organism: Isodon japonicus

enzyme: cycloartenol synthase


organism: Poterioochromonas malhamensis


organism: Archaeoglobus fulgidus


enzyme_display_name: UDP-galactopyranose mutase

organism: Deinococcus radiodurans

substrate_name: UDP-galactopyranose

assay_conditions_summary: pH 7; buffer pH 7

proof_lines: wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0

enzyme: UDP-galactopyranose mutase

substrate: UDP-galactopyranose


organism: Lathyrus oleraceus


organism: Ogataea angusta

proof_lines:
37°C, in presence of 0.1 mM tyrosine
37°C
37°C, in presence of 0.01 mM tryptophan


organism: Corynebacterium glutamicum


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T52P/V55D/L88D with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, mutant enzyme T52P/V55D/L88D


enzyme_display_name: geraniol isomerase

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

substrate_name: linalool

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

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

enzyme: geraniol isomerase

substrate: linalool


organism: Aspergillus fumigatus

substrate_name: UDP-alpha-D-galactofuranose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N207A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant N207A

substrate: UDP-alpha-D-galactofuranose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y104A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant Y104A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y317A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant Y317A


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4W1X2 and applied mutation signature Q107A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for UGM Variants (Biochemistry 2014, 53, 7794-7804); printed column heads mutants | kcat, s-1 | KM (uM) | kcat/KM, M-1 s-1 | relative change. Table 2, AfUGM section, mutant row Q107A; column KM (uM) = 2153; column kcat, s-1 = 4.7; column kcat/KM, M-1 s-1 = 2000; column relative change = 0.003. captured primary segment: UDP-Galf | AfUGMQ107A | Km 2153 uM | kcat 4.7 s^-1 | kcat/Km 2000 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2153 uM; 1 uM is 1/1000 mM, so 2153 / 1000 = 2.153 mM. kcat: printed Table 2 kcat cell 4.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 4.7 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000 / 1000 = 2.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 4.7 / 2.153 = 2.183000464468184 s^-1 mM^-1, alongside the printed catalytic-efficiency cell 2.0 s^-1 mM^-1 that Table 2 fits and reports in its own right.

raw_value_unit_evidence: Table 2, AfUGM section, mutant row Q107A: KM = 2153 uM; kcat = 4.7 s^-1; kcat/KM = 2000 M^-1 s^-1; relative change = 0.003.

status: corrected


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

proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme


organism: Enterobacter agglomerans

substrate_name: chorismate (at 32 degrees Celsius)

column_label: Table 5 reports Erwinia herbicola Km (uM) = 169; table footnote states reaction kinetics were monitored at 32 C.

raw_value_unit_evidence: Km raw_value=169 raw_unit=uM

row_label: Erwinia herbicola

table_label: Table 5 - Kinetic constants, pI and Mw of *AroQ enzymes

substrate: chorismate (at 32 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: isochorismate (for isochorismate pyruvate lyase activity at pH 8 and 37 degrees Celsius)

proof_lines: kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-1) for isochorismate synthase activity (


substrate_name: chorismate (for chorismate mutase activity without magnesium at pH 7.5 and 37 degrees Celsius)


organism: Bacillus subtilis

substrate_name: chorismate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K111N/A112S/V113N to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate

substrate: chorismate


organism: Trypanosoma cruzi

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5EEK1 and applied mutation signature Y100A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for UGM Variants (Biochemistry 2014, 53, 7794-7804); printed column heads mutants | kcat, s-1 | KM (uM) | kcat/KM, M-1 s-1 | relative change. Table 2, TcUGM section, mutant row Y100A; column KM (uM) = 32; column kcat, s-1 = 0.03; column kcat/KM, M-1 s-1 = 800; column relative change = 0.008. captured primary segment: UDP-Galf | TcUGMY100A | Km 32 uM | kcat 0.03 s^-1 | kcat/Km 800 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 32 uM; 1 uM is 1/1000 mM, so 32 / 1000 = 0.032 mM. kcat: printed Table 2 kcat cell 0.03 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.03 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 800 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 800 / 1000 = 0.8 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 0.03 / 0.032 = 0.9375 s^-1 mM^-1, alongside the printed catalytic-efficiency cell 0.8 s^-1 mM^-1 that Table 2 fits and reports in its own right.

raw_value_unit_evidence: Table 2, TcUGM section, mutant row Y100A: KM = 32 uM; kcat = 0.03 s^-1; kcat/KM = 800 M^-1 s^-1; relative change = 0.008.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q103A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant Q103A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y317A to reconstruct the assayed variant sequence.


column_label: Table 2: Steady-State Kinetic Parameters for UGM Variants (Biochemistry 2014, 53, 7794-7804); printed column heads mutants | kcat, s-1 | KM (uM) | kcat/KM, M-1 s-1 | relative change. Table 2, TcUGM section, row Wild-type; column KM (uM) = 140; column kcat, s-1 = 13.4; column kcat/KM, M-1 s-1 = 90000; column relative change = 1. captured primary segment: UDP-Galf | TcUGM wild-type | Km 140 uM | kcat 13.4 s^-1 | kcat/Km 90000 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 140 uM; 1 uM is 1/1000 mM, so 140 / 1000 = 0.14 mM. kcat: printed Table 2 kcat cell 13.4 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.4 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 90000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 90000 / 1000 = 90.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 13.4 / 0.14 = 95.71428571428571 s^-1 mM^-1, alongside the printed catalytic-efficiency cell 90.0 s^-1 mM^-1 that Table 2 fits and reports in its own right.

raw_value_unit_evidence: Table 2, TcUGM section, row Wild-type: KM = 140 uM; kcat = 13.4 s^-1; kcat/KM = 90000 M^-1 s^-1; relative change = 1.

row_label: Table 2, TcUGM section, row Wild-type


organism: Methanocaldococcus jannaschii

proof_lines: kcat is 5.7 sec(-1) (at 30 degrees Celsius).


organism: Escherichia coli (strain K12)

substrate_name: prephenate (at pH 7.8 and at 37 degrees Celsius)

proof_lines: kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.


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

substrate_name: isochorismate (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 1.01 sec(-1) for lyase activity (at pH 7.5 and 22 degrees Celsius). kcat is 23.5 sec(-1) for chorismate mutase activity (at pH 7.5 and 22 degrees Celsius). kcat is 106 min(-1) for lyase activity (at pH 7 and 30 degrees Celsius). kca


organism: Pseudomonas aeruginosa


organism: Aspergillus nidulans

proof_lines: 30°C, pH 7.6, in presence of 0.005 mM tryptophan

proof_lines: 30°C, pH 7.6, in presence of 0.005 mM tyrosine


organism: Mycobacterium tuberculosis


organism: Salmonella typhimurium


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: chorismate (at 30 degrees Celsius)

proof_lines: kcat is 176 sec(-1) for chorismate (PubMed:2187528). kcat is 176 sec(-1) for chorismate (in the presence of 10 uM of tryptophan) (PubMed:2187528). kcat is 348 sec(-1) for chorismate (in the presence of 10 uM of tryptophan and at 30 degrees

substrate: chorismate (at 30 degrees Celsius)


organism: Yersinia pestis

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
kcat is 70 sec(-1).


substrate_name: UDP-D-galactofuranose

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

proof_lines: in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C

source_databases_merged: brenda skid

substrate: UDP-D-galactofuranose


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H131A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 303.15 K; buffer a three-component

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H131A, mutase activity, chorismate column group; column KM (uM) = 53 ± 10; column kcat (s^-1) = 7.2 ± 0.4; column kcat/KM (M^-1 s^-1) = 1.4 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 7.2 s^-1; already in s^-1, no conversion; the exported value is 7.2 s^(-1). Km: printed Table 3 cell 53 uM; 53 / 1000 = 0.053 mM; the exported value is 0.053 mM. kcat/Km: printed Table 3 cell 1.4 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140000.0 / 1000 = 140.0 s^-1 mM^-1; the exported value is 135.8490566037736 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H131A, mutase activity, chorismate column group: KM = 53 ± 10 uM; kcat = 7.2 ± 0.4 s^-1; printed kcat/KM = 1.4 x 10^5 M^-1 s^-1.

table_label: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C (Biochemistry 1998, 37(45):15703-15712)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H153N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H153N, mutase activity, chorismate column group; column KM (uM) = 51 ± 10; column kcat (s^-1) = 10 ± 0.5; column kcat/KM (M^-1 s^-1) = 2.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 10 s^-1; already in s^-1, no conversion; the exported value is 10.0 s^(-1). Km: printed Table 3 cell 51 uM; 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 3 cell 2.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 200000.0 / 1000 = 200.0 s^-1 mM^-1; the exported value is 196.07843137254903 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H153N, mutase activity, chorismate column group: KM = 51 ± 10 uM; kcat = 10 ± 0.5 s^-1; printed kcat/KM = 2.0 x 10^5 M^-1 s^-1.


organism: Leishmania major


enzyme_display_name: 2-methyleneglutarate mutase

organism: Eubacterium barkeri

enzyme: 2-methyleneglutarate mutase


organism: Bos taurus


organism: Aspergillus fumigatus

substrate_name: UDP-alpha-D-galactopyranose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R182A to reconstruct the assayed variant sequence.

substrate: UDP-alpha-D-galactopyranose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R327K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R182K to reconstruct the assayed variant sequence.


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


organism: Arabidopsis thaliana

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

proof_lines: kcat is 16.1 sec(-1) with chorismate as substrate (at pH 8).


proof_lines:
dimeric chorismate mutase, at 20°C
monomeric chorismate mutase, at 20°C


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycosarcoma maydis


organism: Trypanosoma cruzi

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R176A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y395F with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y317F with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R327A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y429F with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


organism: Thermus thermophilus


organism: Pneumocystis carinii

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


proof_lines: pH and temperature not specified in the publication, recombinant mutant F66A


proof_lines: pH 7.0, 25°C, recombinant detagged enzyme


proof_lines: pH and temperature not specified in the publication, recombinant mutant N201A


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q88N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 293.15 K; buffer PBS

proof_lines: mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F77W with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F77W, in PBS buffer (pH 7.5) at 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V35A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V35A, in PBS buffer (pH 7.5) at 20°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme D48G, in PBS buffer (pH 7.5) at 20°C


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

proof_lines: mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20°C


proof_lines: wild type enzyme, in PBS buffer (pH 7.5) at 20°C


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

column_label: Table 5 reports Pseudomonas aeruginosa Km (uM) = 98; table footnote states reaction kinetics were monitored at 32 C.

raw_value_unit_evidence: Km raw_value=98 raw_unit=uM

row_label: Pseudomonas aeruginosa


assay_conditions_summary: pH 8


proof_lines: kcat is 38.7 sec(-1) with chorismate as substrate (at pH 8).


proof_lines: Does not follow Michaelis-Menten kinetics but displays a positive cooperativity with a Hill coefficient of 2.1 indicating that substrate binding at one active site of the homodimer enhances interaction at the second active site (PubMed:2516


organism: Pichia angusta

substrate_name: chorismate (in the presence of 10 uM tryptophan and at 37 degrees Celsius)

column_label: PMC101906 results prose reports that 10 uM tryptophan produced Michaelis-Menten-type kinetics with Km 1.6 mM for chorismate mutase.

raw_value_unit_evidence: Results prose reports Michaelis-Menten-type kinetics with Km raw_value=1.6 raw_unit=mM in the presence of 10 uM tryptophan.

row_label: Purified H. polymorpha HARO7 chorismate mutase with 10 uM tryptophan

table_label: PMC101906 results prose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W315A to reconstruct the assayed variant sequence.


column_label: Table 1 of Biochemistry 2018, 57(26):3713-3721; the printed metric rows are 'kcat (s-1)', 'KM (uM)' and 'kcat/KM (M-1 s-1)'; the enzyme heading read here is 'AfUGM' and the substrate column head under it is 'UDP-Galf'; that column prints kcat 100 s^-1, KM 450 uM and kcat/KM 230000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 100 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; canonical value 100.0 s^(-1). Km: printed Table 1 cell 450 uM; 450 / 1000 = 0.45; canonical value 0.45 mM. kcat/Km: printed Table 1 cell 230000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 230000 / 1000 = 230.0; canonical value 230.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme heading 'AfUGM', substrate column 'UDP-Galf': kcat = 100 s^-1; KM = 450 uM; printed kcat/KM = 230000 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription line for the wild-type AfUGM enzyme with substrate UDP-Galf

table_label: Table 1: Kinetic Parameters for AfUGM and W315A Using UDP-Galf or UDP-Araf as the Substrate (Biochemistry 2018, 57(26):3713-3721)


substrate_name: UDP-beta-L-arabinofuranose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4W1X2 and applied mutation signature W315A to reconstruct the assayed variant sequence.

column_label: Table 1 of Biochemistry 2018, 57(26):3713-3721; the printed metric rows are 'kcat (s-1)', 'KM (uM)' and 'kcat/KM (M-1 s-1)'; the enzyme heading read here is 'W315A' and the substrate column head under it is 'UDP-Araf'; that column prints kcat 0.23 s^-1, KM 700 uM and kcat/KM 331 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.23 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; canonical value 0.23 s^(-1). Km: printed Table 1 cell 700 uM; 700 / 1000 = 0.7; canonical value 0.7 mM. kcat/Km: printed Table 1 cell 331 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 331 / 1000 = 0.331; canonical value 0.331 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme heading 'W315A', substrate column 'UDP-Araf': kcat = 0.23 s^-1; KM = 700 uM; printed kcat/KM = 331 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription line for the W315A variant with substrate UDP-Araf

substrate: UDP-beta-L-arabinofuranose


column_label: Table 1 of Biochemistry 2018, 57(26):3713-3721; the printed metric rows are 'kcat (s-1)', 'KM (uM)' and 'kcat/KM (M-1 s-1)'; the enzyme heading read here is 'AfUGM' and the substrate column head under it is 'UDP-Araf'; that column prints kcat 0.14 s^-1, KM 94 uM and kcat/KM 1540 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.14 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; canonical value 0.14 s^(-1). Km: printed Table 1 cell 94 uM; 94 / 1000 = 0.094; canonical value 0.094 mM. kcat/Km: printed Table 1 cell 1540 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1540 / 1000 = 1.54; canonical value 1.54 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme heading 'AfUGM', substrate column 'UDP-Araf': kcat = 0.14 s^-1; KM = 94 uM; printed kcat/KM = 1540 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription line for the wild-type AfUGM enzyme with substrate UDP-Araf


substrate_name: Chorismate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C216A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C216S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E159A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N160A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q215A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T278A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T278S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T278V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W226A to reconstruct the assayed variant sequence.


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

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


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C88K/R90S to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature C88S/R90K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R90G with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


organism: Chlamydomonas reinhardtii

column_label: Abstract names chorismate mutase EC 5.4.99.5 from Chlamydomonas reinhardi and reports the Michaelis constant for 20-fold purified enzyme was 0.46 mM.

raw_value_unit_evidence: Km raw_value=0.46 mM raw_unit=mM

row_label: Chlamydomonas reinhardtii chorismate mutase / chorismate

table_label: PubMed XML abstract PMID 1122289


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W315A to reconstruct the assayed variant sequence.


source_databases_merged: skid uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R182K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R327K to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM potassium phosphate

column_label: Table One row pKIL10A-W prints CM kcat 0.085 +/- 0.011 s^-1 and CM kcat/Km 2,200 +/- 500 M^-1 s^-1; Table One does not print CM Km.

normalized_value_unit_evidence: kcat=0.085 s^-1; Km=0.038 mM preserved from the exact current source tuple; independently printed kcat/Km=2.2 s^-1 mM^-1; current quotient-derived kcat/Km=2.236842105263158 s^-1 mM^-1.

raw_value_unit_evidence: Table One pKIL10A-W WT PchBH CM cells print kcat 0.085 +/- 0.011 s^-1 and kcat/Km 2,200 +/- 500 M^-1 s^-1; the exact current OED source tuple supplies Km 0.038 mM.

row_label: pKIL10A-W (WT PchBH), CM activity

table_label: Table One. Genetic and kinetic characteristics of representative PchB variants


assay_conditions_summary: pH 7.4; buffer pH 7

column_label: PMID 14678783 kinetic prose, true substrate (3S)-2,3-oxidosqualene, apparent KM = 11 uM; assay method states pH 7.4 and 37 deg C.

raw_value_unit_evidence: The apparent KM and kcat/KM values for the true substrate (3S)-2,3-oxidosqualene were determined to be 11 uM and 1.45 mM^-1 min^-1.

row_label: True substrate (3S)-2,3-oxidosqualene

table_label: Kinetic prose for purified bovine liver oxidosqualene-lanosterol cyclase


organism: Yersinia pestis


organism: Saccharomyces cerevisiae


organism: Ustilago maydis


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.5


organism: Escherichia coli (strain K12)

substrate_name: UDP-GalF

substrate: UDP-GalF


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=37°C, pH=7.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C75A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C75S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


organism: Escherichia coli


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H131A to reconstruct the assayed variant sequence.

row_label: Table 3, protein row H131A, mutase activity, chorismate column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H153N to reconstruct the assayed variant sequence.

row_label: Table 3, protein row H153N, mutase activity, chorismate column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H197N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H197N, mutase activity, chorismate column group; column KM (uM) = 68 ± 10; column kcat (s^-1) = 16 ± 0.5; column kcat/KM (M^-1 s^-1) = 2.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 16 s^-1; already in s^-1, no conversion; the exported value is 16.0 s^(-1). Km: printed Table 3 cell 68 uM; 68 / 1000 = 0.068 mM; the exported value is 0.068 mM. kcat/Km: printed Table 3 cell 2.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 229999.99999999997 / 1000 = 229.99999999999997 s^-1 mM^-1; the exported value is 235.2941176470588 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H197N, mutase activity, chorismate column group: KM = 68 ± 10 uM; kcat = 16 ± 0.5 s^-1; printed kcat/KM = 2.3 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H239N with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H239N, mutase activity, chorismate column group; column KM (uM) = 126 ± 12; column kcat (s^-1) = 2.3 ± 0.1; column kcat/KM (M^-1 s^-1) = 0.18 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.3 s^-1; already in s^-1, no conversion; the exported value is 2.3 s^(-1). Km: printed Table 3 cell 126 uM; 126 / 1000 = 0.126 mM; the exported value is 0.126 mM. kcat/Km: printed Table 3 cell 0.18 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18000.0 / 1000 = 18.0 s^-1 mM^-1; the exported value is 18.253968253968253 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H239N, mutase activity, chorismate column group: KM = 126 ± 12 uM; kcat = 2.3 ± 0.1 s^-1; printed kcat/KM = 0.18 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H245N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H245N, mutase activity, chorismate column group; column KM (uM) = 225 ± 1; column kcat (s^-1) = 4.8 ± 0.1; column kcat/KM (M^-1 s^-1) = 0.21 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.8 s^-1; already in s^-1, no conversion; the exported value is 4.8 s^(-1). Km: printed Table 3 cell 225 uM; 225 / 1000 = 0.225 mM; the exported value is 0.225 mM. kcat/Km: printed Table 3 cell 0.21 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000.0 / 1000 = 21.0 s^-1 mM^-1; the exported value is 21.333333333333332 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H245N, mutase activity, chorismate column group: KM = 225 ± 1 uM; kcat = 4.8 ± 0.1 s^-1; printed kcat/KM = 0.21 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H257A to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H257A, mutase activity, chorismate column group; column KM (uM) = 98 ± 2; column kcat (s^-1) = 8.0 ± 0.5; column kcat/KM (M^-1 s^-1) = 0.81 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 8.0 s^-1; already in s^-1, no conversion; the exported value is 8.0 s^(-1). Km: printed Table 3 cell 98 uM; 98 / 1000 = 0.098 mM; the exported value is 0.098 mM. kcat/Km: printed Table 3 cell 0.81 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 81000.0 / 1000 = 81.0 s^-1 mM^-1; the exported value is 81.63265306122449 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H257A, mutase activity, chorismate column group: KM = 98 ± 2 uM; kcat = 8.0 ± 0.5 s^-1; printed kcat/KM = 0.81 x 10^5 M^-1 s^-1.


sequence_variant_note: Mutation signature H265A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H347N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H347N, mutase activity, chorismate column group; column KM (uM) = 41 ± 8; column kcat (s^-1) = 6.0 ± 0.2; column kcat/KM (M^-1 s^-1) = 1.5 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 6.0 s^-1; already in s^-1, no conversion; the exported value is 6.0 s^(-1). Km: printed Table 3 cell 41 uM; 41 / 1000 = 0.041 mM; the exported value is 0.041 mM. kcat/Km: printed Table 3 cell 1.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150000.0 / 1000 = 150.0 s^-1 mM^-1; the exported value is 146.34146341463415 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H347N, mutase activity, chorismate column group: KM = 41 ± 8 uM; kcat = 6.0 ± 0.2 s^-1; printed kcat/KM = 1.5 x 10^5 M^-1 s^-1.


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

assay_conditions_summary: pH 7.2; 303.15 K; buffer a three-component; cofactor NAD+

column_label: Table label: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 °C. Row: WT. Column group: mutase activity, chorismate. Columns read: KM (µM) cell 45, kcat (s-1) cell 27, kcat/KM (M-1 s-1) cell 6.0 x 10^5. metric: kcat; raw value: 27; raw unit: s^-1; normalized value: 27.0 s^(-1); metric: Km; raw value: 45; raw unit: uM; normalized value: 0.045 mM; metric: kcat/Km; raw value: 6.0 x 10^5; raw unit: M^-1 s^-1; normalized value: 600.0 s^-1 mM^-1; assay condition: Chorismate mutase-prephenate dehydrogenase from E. coli; Table 3 constants measured at pH 7.2 and 30 C; mutase activity was monitored by following the disappearance of chorismate at 274 nm in a three-component buffer of 0.10 M MES, 0.051 M N-ethylmorpholine, 0.051 M diethanolamine (pH 7.2), 1 mM EDTA and 1 mM DTT. Export row conditions: pH 7.2; 303.15 K.

normalized_value_unit_evidence: Mutase-activity/chorismate columns of Table 3, row WT: kcat 27 s^-1 = 27.0 s^(-1); KM 45 µM = 0.045 mM (1 µM = 0.001 mM); kcat/KM 6.0 x 10^5 M^-1 s^-1 = 600.0 s^-1 mM^-1 (1 M^-1 s^-1 = 0.001 mM^-1 s^-1). Rendering quirks of the PDF text extract: superscript exponents are flattened, so the printed cell `6.0 x 10^5` appears as `6.0 × 105` and the header `kcat (s-1)` is the paper's kcat (s^-1); the plus-or-minus sign is extracted as `(`, so `45 ( 7` is the paper's 45 +/- 7 µM; the micro sign renders as µ; and the superscript -1 of the first two column groups is lifted into the separate header line `-1                  -1 -1                    -1                   -1 -1`.

raw_value_unit_evidence: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C | column group header row: mutase activity, chorismate / prephenate / NAD+ (the last two under the spanning header `dehydrogenase activity`); metric header row: `KM (µM)     kcat (s )   kcat/KM (M     s )   KM (µM)     kcat (s )    kcat/KM (M     s )   KM (µM)     kcat (s-1)   kcat/KM (M-1 s-1)` | data row: `WT            45 ( 7   27 ( 0.7          6.0 × 105          44 ( 8  27 ( 1             6.2 × 105         103 ( 11   27 ( 0.7         2.6 × 105` | the three mutase-activity/chorismate cells of the WT row read: KM = 45 µM (printed `45 ( 7`, the `(` being the flattened plus-or-minus sign); kcat = 27 s^-1 (printed `27 ( 0.7`); kcat/KM = 6.0 x 10^5 M^-1 s^-1 (printed `6.0 × 105`).

row_label: WT | mutase activity, chorismate


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


substrate_name: Unknown


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


substrate_name: UDP-L-arabinofuranose

substrate: UDP-L-arabinofuranose


substrate_name: UDP-galactopyranose


mutation_type: deletion

proof_lines: 30°C, pH 7.5, mutant DELTA118-127, with 5.8 mM substrate

proof_lines: 30°C, pH 7.5, mutant DELTA118-127, with 3.4 mM substrate


proof_lines: 30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate


proof_lines: 30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate and DELTA 118-127/R116L/P117T, with 3.9 mM substrate

proof_lines: 30°C, pH 7.5, mutant DELTA118-127/R116L/P117T, with 3.9 mM substrate


organism: Klebsiella pneumoniae

proof_lines: in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C


substrate_name: UDP-D-galactopyranose

substrate: UDP-D-galactopyranose


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


enzyme_display_name: ribonuclease T2

organism: Aspergillus oryzae

substrate_name: ApG

enzyme: ribonuclease T2

substrate: ApG


substrate_name: ApU

substrate: ApU


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


enzyme_display_name: protoporphyrin ferrochelatase

organism: Bdellovibrio bacteriovorus

enzyme: protoporphyrin ferrochelatase


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


proof_lines:
pH 2.6, transphosphorylation
pH 6.7, transphosphorylation
pH 7.2, transphosphorylation


substrate_name: adenylyl (3'-5')uridine

proof_lines:
pH 3.1, transphosphorylation
pH 8.1, transphosphorylation
pH 7.1, transphosphorylation

substrate: adenylyl (3'-5')uridine


enzyme_display_name: prostaglandin-E synthase

organism: Bos taurus

substrate_name: Prostaglandin H1

enzyme: prostaglandin-E synthase

substrate: Prostaglandin H1


substrate_name: Prostaglandin G1

substrate: Prostaglandin G1


substrate_name: chorismate

proof_lines: 30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate


proof_lines: 30°C, pH 7.5, wild-type, with 4 mM substrate


proof_lines:
30°C, pH 7.5, wild-type
30°C, pH 7, wild-type

substrate: Unknown


enzyme_display_name: sirohydrochlorin ferrochelatase

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

enzyme: sirohydrochlorin ferrochelatase


substrate_name: sirohydrochlorin

proof_lines: chimeric mutant enzyme, with Co2+, pH and temperature not specified in the publication

substrate: sirohydrochlorin


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


proof_lines: wild-type enzyme, with Co2+, pH and temperature not specified in the publication


enzyme_display_name: prostaglandin-I synthase

substrate_name: prostaglandin H2

enzyme: prostaglandin-I synthase

substrate: prostaglandin H2


enzyme_display_name: alkylmercury lyase

substrate_name: methyl mercuric chloride

smiles: C[Hg]Cl

enzyme: alkylmercury lyase

substrate: methyl mercuric chloride


substrate_name: n-butyl mercurial

substrate: n-butyl mercurial


substrate_name: phenyl mercuric acetate

substrate: phenyl mercuric acetate


substrate_name: vinylmercuric bromide

substrate: vinylmercuric bromide


substrate_name: cis-2-butenylmercuric chloride

substrate: cis-2-butenylmercuric chloride


substrate_name: UDP-D-galactofuranose

proof_lines: 37°C, pH 7.5, in presence of 20 mM sodium dithionite

substrate: UDP-D-galactofuranose


substrate_name: tetravinyltin

smiles: C=C[Sn](C=C)(C=C)C=C

substrate: tetravinyltin


substrate_name: triethylvinyltin

smiles: CC[Sn](CC)(CC)C=C

substrate: triethylvinyltin


proof_lines: mutant enzyme Glu23Ala, activated by 0.01 mM Trp

substrate: chorismate


proof_lines: mutant enzyme Tyr234Glu, activated by 0.01 mM Trp


proof_lines: mutant enzyme Tyr234Ser, activated by 0.01 mM Trp


proof_lines: mutant enzyme Glu23Gln, activated by 0.01 mM Trp


proof_lines: mutant enzyme Tyr234Ala, activated by 0.01 mM Trp


proof_lines: chorismate, mutant enzyme Thr226Ile, activated by 0.01 mM Trp


proof_lines: wild-type enzyme, activated by 0.01 mM Trp


proof_lines: mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp


proof_lines: mutant enzyme Tyr234Phe, activated by 0.01 mM Trp


proof_lines: mutant enzyme Glu23Asp, activated by 0.01 mM Trp


organism: Sporosarcina pasteurii

substrate_name: phenylmercuric acetate

substrate: phenylmercuric acetate


substrate_name: thiomersol

substrate: thiomersol


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Brassica oleracea

substrate_name: L-cystine

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystine


substrate_name: Unknown


enzyme_display_name: sirohydrochlorin cobaltochelatase

organism: Methanocaldococcus jannaschii

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

enzyme: sirohydrochlorin cobaltochelatase


enzyme_display_name: methionine gamma-lyase

organism: Citrobacter freundii

substrate_name: S-ethyl-L-homocysteine sulfoxide

proof_lines: pH and temperature not specified in the publication

enzyme: methionine gamma-lyase

substrate: S-ethyl-L-homocysteine sulfoxide


substrate_name: S-butyl-L-cysteine

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

substrate: S-butyl-L-cysteine


enzyme_display_name: methylaspartate mutase

organism: Clostridium cochlearium

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

assay_conditions_summary: pH 7

enzyme: methylaspartate mutase


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

assay_conditions_summary: cofactor CoA

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


organism: Clostridium tetanomorphum

substrate_name: L-Glu

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

proof_lines: reaction of L-Glu with benzimidazolribofuranosyl-adenosylcobinamide, fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit

substrate: L-Glu


proof_lines: reaction of L-Glu with benzimidazolribofuranosyl-adenosylcobinamide, wild-type enzyme

proof_lines: reaction with benzimidazolribofuranosyl-adenosylcobinamide, wild-type enzyme and fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit


proof_lines: genetically engineered enzyme with S subunit fused to the C-terminus of the E subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment

proof_lines: genetically engineered enzyme with S subunit fused to the C-terminus of the E-subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment


organism: Cereibacter sphaeroides


substrate_name: deuteroporphyrin

substrate: deuteroporphyrin


organism: Entamoeba histolytica


substrate_name: Glycerate 3-phosphate

proof_lines:
pH 7.0, 37°C
pH 6.0, 37°C
at pH 6.0 and 37°C

substrate: Glycerate 3-phosphate


organism: Cucumis sativus


substrate_name: deuteroporphyrin IX

substrate: deuteroporphyrin IX


enzyme_display_name: D-cysteine desulfhydrase

substrate_name: D-cysteine

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

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


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

proof_lines:
37°C, pH 8.0
30°C, pH 8.0, alpha,beta-elimination


enzyme_display_name: selenocysteine lyase

substrate_name: L-selenocysteine

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

enzyme: selenocysteine lyase

substrate: L-selenocysteine


substrate_name: L-cysteine sulfinate

substrate: L-cysteine sulfinate


enzyme_display_name: protein disulfide-isomerase

substrate_name: scrambled reoxidized lysozyme

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: protein disulfide-isomerase

substrate: scrambled reoxidized lysozyme


substrate_name: Insulin

substrate: Insulin


substrate_name: S-ribosylhomocysteine

substrate: S-ribosylhomocysteine


enzyme_display_name: isochorismate synthase

substrate_name: chorismate

enzyme: isochorismate synthase


proof_lines: wild type enzyme, in 100 mM phosphate pH 7.0, 10 mM MgCl2


enzyme_display_name: chorismate mutase

substrate_name: prephenate

enzyme: chorismate mutase

substrate: prephenate


proof_lines: 37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine

proof_lines: 37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine

proof_lines: 37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine

substrate: chorismate


enzyme_display_name: guanylate cyclase

organism: Drosophila melanogaster

substrate_name: GTP

proof_lines:
with 0.273 mM oxygen
under anaerobic conditions

enzyme: guanylate cyclase

substrate: GTP


substrate: Unknown


enzyme_display_name: phosphopentomutase

substrate_name: deoxyribose 1-phosphate

proof_lines:
enzyme form I
enzyme form II
enzyme form III

enzyme: phosphopentomutase

substrate: deoxyribose 1-phosphate


substrate_name: ribose 1-phosphate

substrate: ribose 1-phosphate


enzyme_display_name: protoporphyrin ferrochelatase

organism: Gallus gallus

substrate_name: protoporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin


enzyme_display_name: S-ribosylhomocysteine lyase

enzyme: S-ribosylhomocysteine lyase


substrate_name: Unknown


organism: Flavobacterium sp.

substrate_name: isochorismate

proof_lines:
enzyme immobilized on alkylamine glass
enzyme immobilized on CNBr-Sepharose
soluble enzyme

substrate: isochorismate


proof_lines:
enzyme immobilized on CNBr-Sepharose
enzyme immobilized on alkylamine glass
soluble enzyme


organism: Fusarium oxysporum

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C

substrate: alpha-D-glucose 1-phosphate


substrate_name: D-glucose 1,6-diphosphate

substrate: D-glucose 1,6-diphosphate


enzyme_display_name: alanine racemase

organism: Aquifex pyrophilus

substrate_name: D-Ala

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

enzyme: alanine racemase

substrate: D-Ala


organism: Thalassiosira sp.

substrate_name: D-alanine

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

substrate: D-alanine


enzyme_display_name: UniProt P10724

organism: Geobacillus stearothermophilus

enzyme: UniProt P10724


enzyme_display_name: UniProt P94556

organism: Bacillus subtilis

substrate_name: L-alanine

enzyme: UniProt P94556

substrate: L-alanine


enzyme_display_name: UniProt P9WPW9

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WPW9


enzyme_display_name: UniProt Q180W0

organism: Clostridioides difficile

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt Q180W0


enzyme_display_name: UniProt Q65YW7

organism: Streptomyces lavendulae

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.2
Raw SKiD Env: Temp=37°C, pH=8.2

enzyme: UniProt Q65YW7


enzyme_display_name: UniProt Q8RAK6

organism: Caldanaerobacter subterraneus subsp. tengcongensis

enzyme: UniProt Q8RAK6


substrate_name: D-Lysine

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

substrate: D-Lysine


enzyme_display_name: UniProt P0A2W8

organism: Streptococcus pneumoniae

enzyme: UniProt P0A2W8


enzyme_display_name: UniProt Q9A1B7

organism: Streptococcus pyogenes

substrate_name: L-glutamate

enzyme: UniProt Q9A1B7

substrate: L-glutamate


enzyme_display_name: UniProt H3ZMH5

organism: Thermococcus litoralis

substrate_name: L-proline

enzyme: UniProt H3ZMH5

substrate: L-proline


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Homo sapiens

substrate_name: beta-chloro-L-alanine

enzyme: cysteine-S-conjugate beta-lyase

substrate: beta-chloro-L-alanine


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


enzyme_display_name: selenocysteine lyase

substrate_name: L-selenocysteine

enzyme: selenocysteine lyase

substrate: L-selenocysteine


enzyme_display_name: prostaglandin-D synthase

substrate_name: glutathione

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

enzyme: prostaglandin-D synthase

substrate: glutathione


enzyme_display_name: lactoylglutathione lyase

proof_lines: pH and temperature not specified in the publication

enzyme: lactoylglutathione lyase


enzyme_display_name: Transferred entry: 4.8.1.2

organism: Pseudomonas chlororaphis

substrate_name: Aldoxime

smiles: C/C=N/O

enzyme: Transferred entry: 4.8.1.2

substrate: Aldoxime


substrate_name: n-Butyraldoxime

smiles: CCC/C=N/O

substrate: n-Butyraldoxime


column_label: Table III; substrate row E/Z-Pyridine-2-aldoxime; columns Km, kcat, and kcat/Km

raw_value_unit_evidence: paper Table III cells: Km=3.4 mM; kcat=0.090 min^-1; kcat/Km=0.026 min^-1 mM^-1

table_label: Table III


enzyme_display_name: L-3-cyanoalanine synthase

organism: Glycine max

substrate_name: L-cysteine

enzyme: L-3-cyanoalanine synthase

substrate: L-cysteine


substrate_name: hydrogen cyanide

substrate: hydrogen cyanide


enzyme_display_name: glutamate racemase

organism: Saccoglossus kowalevskii

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

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

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

enzyme: glutamate racemase


substrate_name: L-aspartate

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

substrate: L-aspartate


proof_lines: mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme


substrate_name: D-glutamate

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme

substrate: D-glutamate


proof_lines: mutant enzyme S156A, pH 8.0, temperature not specified in the publication, AspR enzyme


enzyme_display_name: adenylate cyclase

substrate_name: ATP

assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines:
wild type isoform V, 30°C
wild type isoform VI, 30°C

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: prostaglandin-E synthase

sequence_source: UniProtKB O14684 FASTA

proof_lines: in the presence of 0.3 mM dodecylmaltoside

enzyme: prostaglandin-E synthase


substrate_name: prostaglandine G2

substrate: prostaglandine G2


enzyme_display_name: proline racemase

organism: Ferroplasma acidarmanus

substrate_name: D-proline

enzyme: proline racemase

substrate: D-proline


enzyme_display_name: alanine racemase

organism: Acidiphilium organovorum

substrate_name: D-Ala

assay_conditions_summary: pH 9

enzyme: alanine racemase

substrate: D-Ala


organism: Candidatus Pelagibacter communis

substrate_name: L-alanine

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

substrate: L-alanine


organism: Medicago sativa

substrate_name: D-alanine

proof_lines:
Vmax = 0.44 mol/s/kg
Vmax = 1.02 mol/s/kg

substrate: D-alanine


enzyme_display_name: magnesium dechelatase

organism: Chenopodium album

substrate_name: chlorophyllin a

enzyme: magnesium dechelatase

substrate: chlorophyllin a


organism: Cellana grata


organism: Fragaria x ananassa

assay_conditions_summary: pH 8.8; 310.15 K; buffer only a paper note fragment ('in 50 mM Tris-tricine

proof_lines: in 50 mM Tris-tricine buffer, at 37°C and pH 8.8


substrate_name: L-proline

substrate: L-proline


organism: Tolypocladium inflatum


organism: Bacillus anthracis

substrate_name: Unknown

proof_lines: D-glutamate analog, good competitive inhibitor for RacE1

proof_lines: D-glutamate analog, only weak inhibitor of RacE2

proof_lines: isozyme RacE1, pH and temperature not specified in the publication

substrate: Unknown


organism: Trypanosoma vivax

proof_lines: 40 mM substrate in 0.2 M sodium acetate, for 30 min at 37°C


proof_lines: 0.005 mM pyrrole-2-carboxylic acid, serial concentrations of 20-160 mM L-proline


organism: Aquifex pyrophilus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D7S to reconstruct the assayed variant sequence.


substrate_name: L-glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E147N to reconstruct the assayed variant sequence.

substrate: L-glutamate


enzyme_display_name: coproporphyrin ferrochelatase

organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 0.11 min(-1) with coproporphyrin III as substrate (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate (PubMed:25908396).

enzyme: coproporphyrin ferrochelatase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: coproporphyrin III

proof_lines: kcat is 1.8 min(-1) with coproporphyrin III as substrate. kcat is 0.8 min(-1) with protoporphyrin IX as substrate.

substrate: coproporphyrin III


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


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

substrate_name: cystathionine (at pH 8.8 and 37 degrees Celsius)

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

proof_lines: kcat is 2.3 sec(-1) for cystathionine beta-lyase activity (at pH 8.8 and 37 degrees Celsius). kcat is 3.3 sec(-1) for cystathionine beta-lyase activity (at pH 8.0 and 37 degrees Celsius). kcat is 9.2 sec(-1) for cystathionine beta-lyase act


substrate_name: L-glutamate (at pH 8.0 and 37 degrees Celsius)


organism: Procambarus clarkii


enzyme_display_name: methionine racemase

organism: Thermococcus kodakarensis

substrate_name: L-leucine

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

assay_conditions_summary: pH 5

proof_lines: kcat is 108 sec(-1) with D-leucine as substrate. kcat is 43.3 sec(-1) with L-leucine as substrate. kcat is 86.0 sec(-1) with D-methionine as substrate. kcat is 54.4 sec(-1) with L-methionine as substrate.

enzyme: methionine racemase

substrate: L-leucine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: D-Glutamate

substrate: D-Glutamate


substrate_name: L-Glutamate

substrate: L-Glutamate


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


organism: Lactiplantibacillus plantarum


organism: Pseudomonas aeruginosa

proof_lines:
23°C, enzyme DadX
Raw SKiD Env: Temp=23°C, pH=-----

source_databases_merged: brenda skid uniprot


organism: Wolbachia pipientis

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

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'ALR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 2.3; column 'KM (mM)' = 3.8; column 'kcat/KM (s^-1 M^-1)' = 580. The ALR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.3 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 2.3 s^(-1). Km: printed Table 2 cell 3.8 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 3.8 mM. kcat/Km: printed Table 2 cell 580 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 580 / 1000 = 0.58 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 2.3 / 3.8 = 0.6052631578947368 s^-1 mM^-1, against the printed efficiency cell 0.58 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'ALR', Conditions '37 C, Tris': kcat = 2.3 s^-1; KM = 3.8 mM; printed kcat/KM = 580 s^-1 M^-1.

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


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: Fe(2+) (in the presence of coproporphyrin III)

proof_lines: kcat is 165 min(-1) with coproporphyrin III as substrate. kcat is 15 min(-1) with protoporphyrin IX as substrate.


organism: Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF)

proof_lines: kcat is 64 sec(-1) with L-proline as substrate.


organism: Thermotoga maritima

assay_conditions_summary: pH 8; buffer bicine

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

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


organism: Synechocystis sp. PCC 6803

sequence_variant_note: Mutation signature W385A references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385V references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385I references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385F references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385Y references residue 385, which is outside the resolved sequence length.


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


organism: Mycobacterium avium


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


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Trypanosoma cruzi (strain CL Brener)


organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)

substrate_name: pyridoxal phosphate

proof_lines: kcat is 0.62 sec(-1) with L-leucine as substrate. kcat is 0.79 sec(-1) with D-leucine as substrate. kcat is 1.1 sec(-1) with L-methionine as substrate. kcat is 1.8 sec(-1) with D-methionine as substrate.

substrate: pyridoxal phosphate


organism: Wolbachia pipientis wMel

proof_lines: kcat is 0.001 sec(-1) for cystathionine beta-lyase activity (at pH 8.8 and 37 degrees Celsius). kcat is 2.3 sec(-1) for alanine racemase activity (at pH 8.8 and 37 degrees Celsius). kcat is 0.017 sec(-1) for glutamate racemase activity (at

substrate: cystathionine (at pH 8.8 and 37 degrees Celsius)


substrate_name: L-alanine (at pH 8.8 and 37 degrees Celsius)


organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)


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


organism: Aquifex pyrophilus


organism: Homo sapiens


organism: Clostridioides difficile

proof_lines: substrate: D-proline, Vmax= 0.000017 M/sec

proof_lines: substrate: L-proline, Vmax = 0.000027 M/sec


organism: Caldanaerobacter subterraneus subsp. tengcongensis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S173D with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S173D/Q360Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 10.0, 65°C, recombinant mutant S173D/Q360Y


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q360I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q360Y to reconstruct the assayed variant sequence.


substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q360W to reconstruct the assayed variant sequence.


organism: Wolbachia pipientis

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

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'GLR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 0.017; column 'KM (mM)' = 0.80; column 'kcat/KM (s^-1 M^-1)' = 21. The GLR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.017 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.017 s^(-1). Km: printed Table 2 cell 0.80 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.8 mM. kcat/Km: printed Table 2 cell 21 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 21 / 1000 = 0.021 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 0.017 / 0.80 = 0.02125 s^-1 mM^-1, against the printed efficiency cell 0.021 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'GLR', Conditions '37 C, Tris': kcat = 0.017 s^-1; KM = 0.80 mM; printed kcat/KM = 21 s^-1 M^-1.


enzyme_display_name: sirohydrochlorin nickelchelatase

organism: Methanocaldococcus jannaschii

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

enzyme: sirohydrochlorin nickelchelatase


substrate_name: sirohydrochlorin

proof_lines: wild-type enzyme, with Ni2+, pH and temperature not specified in the publication

substrate: sirohydrochlorin


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

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


proof_lines: chimeric mutant enzyme, with Ni2+, pH and temperature not specified in the publication


organism: Escherichia coli

substrate_name: L-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D164K to reconstruct the assayed variant sequence.

substrate: L-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E165A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

column_label: Table 2, enzyme row 'E165A', L- to D-Ala block; column 'Km (mM)' = 1.562 ± 0.256; column 'kcat (min-1)' = 1348 ± 160; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1348 min-1; min^-1 to s^-1 is a division by 60, so 1348 / 60 = 22.466666666666665 s^(-1); the exported value 22.467 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.562 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.562 mM; the exported value is 1.562 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 14.383269312846776 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 22.466666666666665 / 1.562 of this row's own two printed cells, typed derived_same_measurement; the exported value 14.383482714468629 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E165A', L- to D-Ala block: kcat = 1348 min-1; Km (mM) = 1.562 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E165A', L- to D-Ala direction

table_label: Table 2: Kinetic parameters of the wild-type EcAlr and its mutants (Protein Science 2008, 17:1066-1076)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E165K to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E165K', L- to D-Ala block; column 'Km (mM)' = 2.057 ± 0.038; column 'kcat (min-1)' = 1003 ± 51; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1003 min-1; min^-1 to s^-1 is a division by 60, so 1003 / 60 = 16.716666666666665 s^(-1); the exported value 16.717 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 2.057 mM; the cell is already in mM, so no unit conversion applies and the paper value is 2.057 mM; the exported value is 2.057 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 8.1267217630854 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 16.716666666666665 / 2.057 of this row's own two printed cells, typed derived_same_measurement; the exported value 8.126883811375789 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E165K', L- to D-Ala block: kcat = 1003 min-1; Km (mM) = 2.057 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E165K', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E221A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E221A', L- to D-Ala block; column 'Km (mM)' = 1.516 ± 0.083; column 'kcat (min-1)' = 4255 ± 140; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4255 min-1; min^-1 to s^-1 is a division by 60, so 4255 / 60 = 70.91666666666667 s^(-1); the exported value 70.917 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.516 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.516 mM; the exported value is 1.516 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 46.7788038698329 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 70.91666666666667 / 1.516 of this row's own two printed cells, typed derived_same_measurement; the exported value 46.779023746701846 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221A', L- to D-Ala block: kcat = 4255 min-1; Km (mM) = 1.516 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221A', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E221K to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E221K', L- to D-Ala block; column 'Km (mM)' = 1.993 ± 0.269; column 'kcat (min-1)' = 4094 ± 453; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4094 min-1; min^-1 to s^-1 is a division by 60, so 4094 / 60 = 68.23333333333333 s^(-1); the exported value 68.233 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.993 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.993 mM; the exported value is 1.993 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 34.23649439705636 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 68.23333333333333 / 1.993 of this row's own two printed cells, typed derived_same_measurement; the exported value 34.23632714500753 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221K', L- to D-Ala block: kcat = 4094 min-1; Km (mM) = 1.993 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221K', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E221P to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E221P', L- to D-Ala block; column 'Km (mM)' = 1.401 ± 0.209; column 'kcat (min-1)' = 4024 ± 458; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4024 min-1; min^-1 to s^-1 is a division by 60, so 4024 / 60 = 67.06666666666666 s^(-1); the exported value 67.067 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.401 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.401 mM; the exported value is 1.401 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 47.87056864144658 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 67.06666666666666 / 1.401 of this row's own two printed cells, typed derived_same_measurement; the exported value 47.87080656673804 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221P', L- to D-Ala block: kcat = 4024 min-1; Km (mM) = 1.401 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221P', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature P219A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'P219A', L- to D-Ala block; column 'Km (mM)' = 1.049 ± 0.131; column 'kcat (min-1)' = 3106 ± 364; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3106 min-1; min^-1 to s^-1 is a division by 60, so 3106 / 60 = 51.766666666666666 s^(-1); the exported value 51.767 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.049 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.049 mM; the exported value is 1.049 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 49.34858595487766 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 51.766666666666666 / 1.049 of this row's own two printed cells, typed derived_same_measurement; the exported value 49.34890371782651 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'P219A', L- to D-Ala block: kcat = 3106 min-1; Km (mM) = 1.049 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'P219A', L- to D-Ala direction


substrate_name: D-alanine


substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature D164A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: Table 2, enzyme row 'D164A', D- to L-Ala block; column 'Km (mM)' = 0.615 ± 0.032; column 'kcat (min-1)' = 268 ± 12; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 268 min-1; min^-1 to s^-1 is a division by 60, so 268 / 60 = 4.466666666666667 s^(-1); the exported value 4.467 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.615 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.615 mM; the exported value is 0.615 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 7.262872628726288 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.466666666666667 / 0.615 of this row's own two printed cells, typed derived_same_measurement; the exported value 7.263414634146341 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'D164A', D- to L-Ala block: kcat = 268 min-1; Km (mM) = 0.615 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'D164A', D- to L-Ala direction

substrate: D-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature D164K to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'D164K', D- to L-Ala block; column 'Km (mM)' = 0.604 ± 0.070; column 'kcat (min-1)' = 20 ± 2; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 20 min-1; min^-1 to s^-1 is a division by 60, so 20 / 60 = 0.3333333333333333 s^(-1); the exported value 0.333 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.604 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.604 mM; the exported value is 0.604 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.5518763796909492 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.3333333333333333 / 0.604 of this row's own two printed cells, typed derived_same_measurement; the exported value 0.5513245033112584 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'D164K', D- to L-Ala block: kcat = 20 min-1; Km (mM) = 0.604 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'D164K', D- to L-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


column_label: Table 2, enzyme row 'E165K', D- to L-Ala block; column 'Km (mM)' = 0.528 ± 0.079; column 'kcat (min-1)' = 79 ± 6; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 79 min-1; min^-1 to s^-1 is a division by 60, so 79 / 60 = 1.3166666666666667 s^(-1); the exported value 1.317 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.528 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.528 mM; the exported value is 0.528 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 2.4936868686868685 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.3166666666666667 / 0.528 of this row's own two printed cells, typed derived_same_measurement; the exported value 2.4943181818181817 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E165K', D- to L-Ala block: kcat = 79 min-1; Km (mM) = 0.528 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E165K', D- to L-Ala direction


column_label: Table 2, enzyme row 'E221A', D- to L-Ala block; column 'Km (mM)' = 0.439 ± 0.080; column 'kcat (min-1)' = 409 ± 39; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 409 min-1; min^-1 to s^-1 is a division by 60, so 409 / 60 = 6.816666666666666 s^(-1); the exported value 6.817 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.439 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.439 mM; the exported value is 0.439 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 15.527714502657554 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.816666666666666 / 0.439 of this row's own two printed cells, typed derived_same_measurement; the exported value 15.528473804100228 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221A', D- to L-Ala block: kcat = 409 min-1; Km (mM) = 0.439 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221A', D- to L-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E221K to reconstruct the assayed variant sequence.


column_label: Table 2, enzyme row 'E221P', D- to L-Ala block; column 'Km (mM)' = 0.513 ± 0.084; column 'kcat (min-1)' = 457 ± 45; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 457 min-1; min^-1 to s^-1 is a division by 60, so 457 / 60 = 7.616666666666666 s^(-1); the exported value 7.617 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.513 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.513 mM; the exported value is 0.513 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 14.84730344379467 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 7.616666666666666 / 0.513 of this row's own two printed cells, typed derived_same_measurement; the exported value 14.847953216374268 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221P', D- to L-Ala block: kcat = 457 min-1; Km (mM) = 0.513 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221P', D- to L-Ala direction