proof_lines: mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


enzyme_display_name: xylose isomerase

organism: Streptomyces pseudogriseolus

substrate_name: D-xylose

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

enzyme: xylose isomerase

substrate: D-xylose

source: brenda


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

mutation_type: substitution

proof_lines: mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


enzyme_display_name: L-arabinose isomerase

organism: Bacillus licheniformis

substrate_name: L-arabinose

verification_status: unverified

enzyme: L-arabinose isomerase

substrate: L-arabinose

status: unverified


proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme


organism: Geobacillus stearothermophilus

kcat_display: Not reported


substrate_name: L-fucose

substrate: L-fucose


enzyme_display_name: ribose-5-phosphate isomerase

organism: Brucella anthropi

substrate_name: D-allose

enzyme: ribose-5-phosphate isomerase

substrate: D-allose


proof_lines: recombinant mutant S9T/S98H/S134H, pH 7.5, 50°C


proof_lines: recombinant mutant S98H/S134H, pH 7.5, 50°C


enzyme_display_name: mannose-6-phosphate isomerase

organism: Thermus thermophilus

substrate_name: L-ribulose

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

enzyme: mannose-6-phosphate isomerase

substrate: L-ribulose


organism: Bacillus subtilis

substrate_name: D-ribose

substrate: D-ribose


substrate_name: L-allose

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

substrate: L-allose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: L-ribose

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

substrate: L-ribose


organism: Actinoplanes missouriensis

proof_lines:
wild-type
wild-type enzyme


substrate_name: D-glucose

substrate: D-glucose


organism: Clostridioides difficile

substrate_name: L-talose

substrate: L-talose


proof_lines:
pH 7.5 and 40°C
pH 7.5, 40°C


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


organism: Streptomyces olivochromogenes

substrate_name: xylulose

substrate: xylulose


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: glucose-6-phosphate isomerase

organism: Archaeoglobus fulgidus

substrate_name: D-fructose 6-phosphate

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

enzyme: glucose-6-phosphate isomerase

substrate: D-fructose 6-phosphate


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Geobacillus thermodenitrificans


substrate_name: D-galactose

proof_lines:
mutant C450S/N475K, pH 8, 55°C
C450S /N475K mutant

substrate: D-galactose


substrate_name: L-arabinose

substrate: L-arabinose


organism: Escherichia coli


organism: Arthrobacter sp.

substrate_name: D-Lyxose

proof_lines:
30°C
D-xylose, with 30 mM Mg2+
D-xylose, 30°C

substrate: D-Lyxose


organism: Homo sapiens

substrate_name: fructose 6-phosphate

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

proof_lines:
mutant enzyme Thr224 to Met
mutant enzyme Thr5 to Ile
mutant enzyme Asp539 to Asn

substrate: fructose 6-phosphate


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


proof_lines: in the presence of 10 mM Mn2+, enzyme treated with EDTA

proof_lines: in the presence of 1 mM Mn2+, enzyme treated with EDTA


organism: Methanosarcina mazei


organism: Oryctolagus cuniculus

proof_lines: muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors


organism: Sinorhizobium meliloti


organism: Spinacia oleracea

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


organism: Streptomyces sp.


substrate_name: D-xylose

substrate: D-xylose


organism: Streptomyces albus


substrate_name: L-rhamnose

substrate: L-rhamnose


organism: Thermoanaerobacterium saccharolyticum


organism: Lactococcus lactis


organism: Thermus thermophilus

substrate_name: D-mannose

substrate: D-mannose


proof_lines:
wild type enzyme, at pH 7.0 and 85°C
60°C, pH 7, wild-type


organism: Alicyclobacillus acidocaldarius

proof_lines:
pH 6.0, 65°C, recombinant enzyme
pH 7.5, 75°C, recombinant enzyme


organism: Alicyclobacillus hesperidum


organism: Salmonella enterica


proof_lines:
wild-type at pH 8 and 65°C
wild-type at pH 7 and 65°C
wild-type at pH 6 and 65°C


organism: Anoxybacillus flavithermus

assay_conditions_summary: pH 9.5; 368.15 K; buffer 50 mM glycine-NaOH

proof_lines: in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C


proof_lines: without borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C

proof_lines: with 10 mM borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C


organism: Bacillus subtilis

substrate_name: L-aldose

proof_lines: pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme

substrate: L-aldose


substrate_name: L-ribulose

substrate: L-ribulose


organism: Bacillus sp. (in: firmicutes)

substrate_name: D-glucose

substrate: D-glucose


organism: Bifidobacterium adolescentis


organism: Bifidobacterium longum

proof_lines:
at pH 6.5 and 45°C
pH 6.0-6.5, 55°C, recombinant enzyme


organism: Candida albicans

substrate_name: mannose 6-phosphate

assay_conditions_summary: buffer selenomethionine-labelled enzyme Hepes buffer selenomethionine-labelled enzyme

proof_lines: selenomethionine-labelled enzyme, Hepes buffer

substrate: mannose 6-phosphate


organism: Brucella anthropi

substrate_name: D-allose

proof_lines: pH 7.5, 45°C, recombinant wild-type enzyme

proof_lines: pH 7.0, 45°C, recombinant wild-type enzyme

proof_lines: recombinant wild-type enzyme, pH 7.5, 50°C

substrate: D-allose


proof_lines: pH 7.5, 45°C, recombinant mutant A10T/T32S/G101N


organism: Bacteroides stercoris

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM Tris-HCl

proof_lines: in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30°C


substrate_name: D-mannose 6-phosphate

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

substrate: D-mannose 6-phosphate


organism: Cricetulus griseus


organism: Enterococcus faecium

proof_lines:
at pH 7.0 and 50°C
pH 7.0-7.5, 45-50°C, recombinant enzyme


organism: Escherichia coli

substrate_name: D-ribose 5-phosphate

proof_lines:
ribosephosphate isomerase B
ribosephosphate isomerase A

substrate: D-ribose 5-phosphate


substrate_name: beta-D-mannose 6-phosphate

assay_conditions_summary: pH 7.1; 298.15 K; buffer 50 mM HEPES

proof_lines:
in 50 mM HEPES buffer, pH 7.1, at 25°C
22°C, pH 7.4

substrate: beta-D-mannose 6-phosphate


substrate_name: Unknown

proof_lines:
in 50 mM HEPES buffer, pH 7.1, at 25°C
pH 7.1, 25°C, recombinant enzyme

substrate: Unknown


substrate_name: D-tagatose

proof_lines:
pH 7.0, 37°C, purified enzyme
pH 7.0, 37°C, whole cells

substrate: D-tagatose


substrate_name: D-galactose

substrate: D-galactose


organism: Geobacillus stearothermophilus

proof_lines: pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis


substrate_name: L-arabinose

proof_lines: in the presence of 0.8 mM Mn2+, at pH 7.5 and 60°C

substrate: L-arabinose


proof_lines: without borate, pH 8.0, 60°C, recombinant wild-type enzyme

proof_lines: with borate, pH 8.0, 60°C, recombinant wild-type enzyme


proof_lines: pH 8.0, 60°C, recombinant wild-type enzyme


organism: Geobacillus kaustophilus


substrate_name: D-xylulose

substrate: D-xylulose


substrate_name: D-fructose

substrate: D-fructose


organism: Halalkalibacterium halodurans


organism: Heyndrickxia coagulans

substrate_name: D-xylose

substrate: D-xylose


organism: Homo sapiens

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


organism: Klebsiella aerogenes


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Lactiplantibacillus plantarum

substrate_name: L-ribulose

substrate: L-ribulose


proof_lines:
at 60°C, pH 7.5
pH 7.5, 60°C, recombinant enzyme


organism: Lentilactobacillus parabuchneri


organism: Latilactobacillus sakei

assay_conditions_summary: pH 5; buffer 100 mM sodium acetate

proof_lines: with 0.8 mM MgCl2 and 0.8 mM MnCl2, in 100 mM sodium acetate buffer (pH 5.0), at 35°C


proof_lines:
wild-type at pH 6 and 50°C
wild-type at pH 7 and 50°C
wild-type at pH 8 and 50°C


proof_lines:
mutant E268K at pH 6 and 50°C
mutant E268K at pH 8 and 50°C
mutant E268K at pH 7 and 50°C


organism: Limosilactobacillus fermentum

assay_conditions_summary: pH 6.5; 338.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C


organism: Levilactobacillus brevis

substrate_name: D-ribose

substrate: D-ribose


substrate_name: D-glucose

substrate: D-glucose


organism: Mus musculus

substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Limosilactobacillus reuteri


organism: Piromyces sp.

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


proof_lines: mutant enzyme E129D/V433I, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


enzyme_display_name: glutamate racemase

organism: Pediococcus pentosaceus

substrate_name: L-Glu

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

enzyme: glutamate racemase

substrate: L-Glu


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


organism: Lathyrus oleraceus

substrate_name: D-ribulose 5-phosphate

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

substrate: D-ribulose 5-phosphate


organism: Saccharomyces cerevisiae

substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


substrate_name: Unknown

proof_lines:
pH 7.1, 25°C
pH 7.1, 25°C, recombinant enzyme

substrate: Unknown


organism: Pseudomonas aeruginosa


assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM HEPES

proof_lines:
in 50 mM HEPES buffer, pH 7.1, at 25°C
pH 8.0


proof_lines: values of 0.27 mM, 0.3 mM, 0.7 mM, 0.8 mM and 1.5 mM are determined by different authors


organism: Streptomyces pseudogriseolus

substrate_name: D-glyceraldehyde

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

proof_lines: in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C

substrate: D-glyceraldehyde


organism: Streptomyces sp. 32


organism: Streptomyces sp. 1


organism: Shewanella sp. ANA-3

substrate_name: L-arabinose

substrate: L-arabinose


substrate_name: D-galactose

substrate: D-galactose


organism: Thermotoga petrophila


substrate_name: alpha-D-xylopyranose

substrate: alpha-D-xylopyranose


enzyme_display_name: protein disulfide-isomerase

organism: Triticum aestivum

substrate_name: ribonuclease

enzyme: protein disulfide-isomerase

substrate: ribonuclease


organism: Thermus thermophilus


organism: Arabidopsis thaliana


organism: Thermotoga neapolitana

protein_accession_database: UniProt

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

proof_lines:
pH 7.0, 85°C
pH 7.0, 85°C, recombinant enzyme

data_origin: experimental


organism: Bacillus amyloliquefaciens


organism: Bacillus cereus

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

proof_lines: in presence of 0.5 mM UDP-N-acetylglucosamine

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


organism: Vibrio sp.

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer (pH 7.5), at 40°C


substrate_name: D-xylose

substrate: D-xylose


enzyme_display_name: phosphopentomutase

proof_lines: in 25 mM Tris-HCl, pH 8.0, and 0.1 mM MnCl2, 0.0005 mM glucose 1,6-bisphosphate,at 23°C

enzyme: phosphopentomutase


organism: Bacillus licheniformis

assay_conditions_summary: pH 7.5; 323.15 K; buffer 50 mM phosphate

proof_lines: pH and temperature not specified in the publication

proof_lines: immobilized enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C


enzyme_display_name: L-rhamnose isomerase

organism: Thermobacillus composti

substrate_name: L-rhamnose

enzyme: L-rhamnose isomerase

substrate: L-rhamnose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: D-psicose

substrate: D-psicose


substrate_name: D-allose

substrate: D-allose


enzyme_display_name: UniProt Q75WH8

organism: Pseudomonas stutzeri

substrate_name: D-ribose

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=35°C, pH=9
Raw SKiD Env: Temp=50°C, pH=9

enzyme: UniProt Q75WH8

substrate: D-ribose

source: skid


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=35°C, pH=9
Raw SKiD Env: Temp=50°C, pH=9


substrate_name: L-Lyxose

substrate: L-Lyxose


organism: Bacillus subtilis

source_db: oed

source: oed


substrate_name: L-Rhamnose

substrate: L-Rhamnose


enzyme_display_name: D-lyxose ketol-isomerase

organism: Paenibacillus baekrokdamisoli

substrate_name: D-allulose

enzyme: D-lyxose ketol-isomerase

substrate: D-allulose


organism: Thermosediminibacter oceani

substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: D-Mannose

substrate: D-Mannose


proof_lines: pH 7, 25°C, in presence of dihexanoylphosphatidylcholine

proof_lines: pH 7, 25°C, in absence of dihexanoylphosphatidylcholine


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-lysine

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

enzyme: lysine 2,3-aminomutase

substrate: L-lysine


enzyme_display_name: beta-phosphoglucomutase

substrate_name: beta-D-glucose 1-phosphate

proof_lines:
phosphoglucomutase activity
1-phosphate phosphodismutase activity

enzyme: beta-phosphoglucomutase

substrate: beta-D-glucose 1-phosphate


organism: Arthrobacter sp.

substrate_name: D-galactose

substrate: D-galactose


enzyme_display_name: ribulose-phosphate 3-epimerase

organism: Bacillus methanolicus

substrate_name: D-ribulose 5-phosphate

enzyme: ribulose-phosphate 3-epimerase

substrate: D-ribulose 5-phosphate


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


proof_lines:
Fe2+ containing BsLuxS
Co2+ substituted BsLuxS
native enzyme


organism: Stutzerimonas stutzeri

assay_conditions_summary: pH 9; 308.15 K; buffer 50 mM glycine-NaOH

proof_lines: mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


enzyme_display_name: glucuronate isomerase

organism: Escherichia coli

substrate_name: D-Glucuronate

enzyme: glucuronate isomerase

substrate: D-Glucuronate


substrate_name: L-rhamnose

substrate: L-rhamnose


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


substrate_name: L-Xylose

substrate: L-Xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-altrose

substrate: D-altrose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-rhamnulose

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

substrate: L-rhamnulose


organism: Thermotoga maritima

assay_conditions_summary: pH 8; 358.15 K; buffer 50 mM EPPS

proof_lines: purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)


substrate_name: L-Fructose

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

substrate: L-Fructose


substrate_name: L-xylulose

substrate: L-xylulose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: L-Lyxose

substrate: L-Lyxose


organism: Thermoprotei archaeon

substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: L-ribose

substrate: L-ribose


enzyme_display_name: arabinose-5-phosphate isomerase

organism: Acidipropionibacterium acidipropionici

substrate_name: D-arabinose 5-phosphate

enzyme: arabinose-5-phosphate isomerase

substrate: D-arabinose 5-phosphate


substrate_name: D-allose

substrate: D-allose


proof_lines: mutant enzyme H101N, pH and temperature not specified in the publication


organism: Clostridium tetani

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Caldanaerobius polysaccharolyticus


organism: Thermoflavimicrobium dichotomicum


substrate_name: L-rhamnose

proof_lines: 50°C, pH 9.0, intrinsic enzyme from Pseudomonas stutzeri

substrate: L-rhamnose


organism: Thermofilum sp. ex4484_79

sequence_source: multiple

assay_conditions_summary: pH 7

source_databases_merged: brenda uniprot


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: ProFAR

source_db: uniprot

substrate: ProFAR

source: uniprot


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature R83N to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'R83N tHisA'; metric row kcat (s-1) = 0.23; metric row KmProFAR (uM) = 37.9; metric row kcat/KmProFAR (uM-1 s-1) = 0.006. captured primary segment: R83N tHisA | kcat 0.23 s^-1 | Km(ProFAR) 37.9 uM | kcat/Km(ProFAR) 0.006 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.23 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.23 s^(-1). Km: printed Table 3 cell 37.9 uM; 1 uM is 1/1000 mM, so 37.9 / 1000 = 0.0379 mM. kcat/Km: printed Table 3 cell 0.006 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.006 x 1000 = 6.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'R83N tHisA': kcat = 0.23 s^-1; Km(ProFAR) = 37.9 uM; printed kcat/Km(ProFAR) = 0.006 uM^-1 s^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature D127N to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'D127N tHisA'; metric row kcat (s-1) = 0.00027; metric row KmProFAR (uM) = 2.0; metric row kcat/KmProFAR (uM-1 s-1) = 0.00013. captured primary segment: D127N tHisA | kcat 0.00027 s^-1 | Km(ProFAR) 2.0 uM | kcat/Km(ProFAR) 0.00013 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.00027 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.00027 s^(-1). Km: printed Table 3 cell 2.0 uM; 1 uM is 1/1000 mM, so 2.0 / 1000 = 0.002 mM. kcat/Km: printed Table 3 cell 0.00013 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.00013 x 1000 = 0.13 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'D127N tHisA': kcat = 0.00027 s^-1; Km(ProFAR) = 2.0 uM; printed kcat/Km(ProFAR) = 0.00013 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature H48A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'H48A tHisA'; metric row kcat (s-1) = 0.38; metric row KmProFAR (uM) = 2.9; metric row kcat/KmProFAR (uM-1 s-1) = 0.131. captured primary segment: H48A tHisA | kcat 0.38 s^-1 | Km(ProFAR) 2.9 uM | kcat/Km(ProFAR) 0.131 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.38 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.38 s^(-1). Km: printed Table 3 cell 2.9 uM; 1 uM is 1/1000 mM, so 2.9 / 1000 = 0.0029 mM. kcat/Km: printed Table 3 cell 0.131 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.131 x 1000 = 131.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'H48A tHisA': kcat = 0.38 s^-1; Km(ProFAR) = 2.9 uM; printed kcat/Km(ProFAR) = 0.131 uM^-1 s^-1.


proof_lines:
25°C, pH 7.5, wild-type enzyme
37°C, pH 7.5, wild-type enzyme
80°C, pH 7.5, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature T164A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'T164A tHisA'; metric row kcat (s-1) = 0.018; metric row KmProFAR (uM) = 5.6; metric row kcat/KmProFAR (uM-1 s-1) = 0.003. captured primary segment: T164A tHisA | kcat 0.018 s^-1 | Km(ProFAR) 5.6 uM | kcat/Km(ProFAR) 0.003 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.018 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.018 s^(-1). Km: printed Table 3 cell 5.6 uM; 1 uM is 1/1000 mM, so 5.6 / 1000 = 0.0056 mM. kcat/Km: printed Table 3 cell 0.003 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.003 x 1000 = 3.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'T164A tHisA': kcat = 0.018 s^-1; Km(ProFAR) = 5.6 uM; printed kcat/Km(ProFAR) = 0.003 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature D51N to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'D51N tHisA'; metric row kcat (s-1) = 0.29; metric row KmProFAR (uM) = 6.4; metric row kcat/KmProFAR (uM-1 s-1) = 0.046. captured primary segment: D51N tHisA | kcat 0.29 s^-1 | Km(ProFAR) 6.4 uM | kcat/Km(ProFAR) 0.046 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.29 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.29 s^(-1). Km: printed Table 3 cell 6.4 uM; 1 uM is 1/1000 mM, so 6.4 / 1000 = 0.0064 mM. kcat/Km: printed Table 3 cell 0.046 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.046 x 1000 = 46.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'D51N tHisA': kcat = 0.29 s^-1; Km(ProFAR) = 6.4 uM; printed kcat/Km(ProFAR) = 0.046 uM^-1 s^-1.


organism: Bacteroides fragilis

substrate_name: Unknown

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

substrate: Unknown


organism: Escherichia coli (strain K12)


organism: Cohnella laeviribosi


organism: Escherichia coli O157:H7

proof_lines: kcat is 13.7 sec(-1) with D-lyxose as substrate. kcat is 12.7 sec(-1) with D-mannose as substrate. kcat is 8.78 sec(-1) with L-gulose as substrate.


organism: Serratia proteamaculans

column_label: Table 1 (Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates) carries the columns Substrate | Product | Specific activity (umol min^-1 mg^-1) | Km (mmol l^-1) | kcat (s^-1) | kcat/Km ((mmol l^-1)^-1 s^-1), with the substrate rows grouped under the block labels Aldose, Ketose and Aldose phosphate. The cited cell set is the Aldose block, substrate row D-Lyxose (product D-Xylulose): Specific activity (umol min^-1 mg^-1) = 10.0; Km (mmol l^-1) = 13.3; kcat (s^-1) = 30 810; kcat/Km ((mmol l^-1)^-1 s^-1) = 2333.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.3 under the column head Km (mmol l^-1); 1 mmol l^-1 is 1 mM, so no unit conversion applies and the paper value is 13.3 mM. kcat: printed Table 1 cell 30 810 under the column head kcat (s^-1); the thousands space is typography and the cell reads 30810; the column is already in s^-1, so no unit conversion applies and the paper value is 30810.0 s^(-1). kcat/Km: printed Table 1 cell 2333 under the column head kcat/Km ((mmol l^-1)^-1 s^-1); 1 (mmol l^-1)^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 2333.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Aldose block, substrate row D-Lyxose (product D-Xylulose): Km = 13.3 mmol l^-1; kcat = 30 810 s^-1 (printed with a thousands space); printed kcat/Km = 2333 (mmol l^-1)^-1 s^-1.

table_label: Table 1: Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates (Letters in Applied Microbiology 51 (2010) 343-350)


proof_lines: kcat is 30810 sec(-1) with D-lyxose as substrate. kcat is 16170 sec(-1) with D-mannose as substrate. kcat is 31620 sec(-1) with D-xylulose as substrate. kcat is 4297 sec(-1) with D-fructose as substrate.


organism: Mesorhizobium loti

substrate_name: D-ribose

assay_conditions_summary: pH 9

proof_lines: in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C

substrate: D-ribose


substrate_name: L-talose; L-mannose

substrate: L-talose; L-mannose


substrate_name: L-lyxose

substrate: L-lyxose


substrate_name: D-Mannose

assay_conditions_summary: pH 7.5; 313.15 K; buffer 50 mmol/L EPPS

normalized_value_unit_evidence: paper normalized kcat_over_km=502 s^-1*mM^-1; expected normalized value 502.1739130434782 s^-1*mM^-1 agrees by table rounding/SD

row_label: D-Mannose -> D-Fructose

table_label: Table 1: Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates

substrate: D-Mannose


substrate_name: D-xylulose

column_label: Table 1 (Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates) carries the columns Substrate | Product | Specific activity (umol min^-1 mg^-1) | Km (mmol l^-1) | kcat (s^-1) | kcat/Km ((mmol l^-1)^-1 s^-1), with the substrate rows grouped under the block labels Aldose, Ketose and Aldose phosphate. The cited cell set is the Ketose block, substrate row D-Xylulose (product D-Lyxose): Specific activity (umol min^-1 mg^-1) = 26.2; Km (mmol l^-1) = 3.83; kcat (s^-1) = 31 620; kcat/Km ((mmol l^-1)^-1 s^-1) = 9560.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.83 under the column head Km (mmol l^-1); 1 mmol l^-1 is 1 mM, so no unit conversion applies and the paper value is 3.83 mM. kcat: printed Table 1 cell 31 620 under the column head kcat (s^-1); the thousands space is typography and the cell reads 31620; the column is already in s^-1, so no unit conversion applies and the paper value is 31620.0 s^(-1). kcat/Km: printed Table 1 cell 9560 under the column head kcat/Km ((mmol l^-1)^-1 s^-1); 1 (mmol l^-1)^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 9560.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Ketose block, substrate row D-Xylulose (product D-Lyxose): Km = 3.83 mmol l^-1; kcat = 31 620 s^-1 (printed with a thousands space); printed kcat/Km = 9560 (mmol l^-1)^-1 s^-1.

substrate: D-xylulose


substrate_name: D-lyxose

row_label: Table 1, Aldose block, substrate row D-Lyxose

substrate: D-lyxose


substrate_name: D-Xylulose

column_label: Table 1 row D-Xylulose -> D-Lyxose, primary kcat/Km column: 9560 +/- 34 ((mmol l^-1)^-1 s^-1), not the current 8255.874673629243 s^-1 mM^-1.

normalized_value_unit_evidence: Km 3.83 mM; kcat 31620 s^-1; explicit kcat/Km 9560 s^-1 mM^-1.

row_label: D-Xylulose -> D-Lyxose

table_label: Table 1. Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates

substrate: D-Xylulose


organism: Thermofilum sp. (strain ex4484_79)


organism: Thermosediminibacter oceani

proof_lines: kcat is 3108 min(-1) with D-lyxose as substrate. kcat is 5686 min(-1) with D-mannose as substrate. kcat is 1030 min(-1) with D-fructose as substrate.


organism: Dictyoglomus turgidum

assay_conditions_summary: pH 8


substrate_name: L-Fructose

substrate: L-Fructose


substrate_name: L-xylulose

substrate: L-xylulose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: L-Lyxose

substrate: L-Lyxose


verification_status: verified

assay_conditions_summary: pH 8; 348.15 K; buffer 50 mM EPPS

column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row D-Allose: column Km (mM) = 61.5; column kcat (s-1) = 81; column kcat/Km (mM-1 s-1) = 1.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 61.5 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 61.5 mM. kcat: printed Table 1 cell 81 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 81.0 s^(-1). kcat/Km: printed Table 1 cell 1.3 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 1.3 s^(-1)*mM^(-1). Quotient disclosure for this row: 81 / 61.5 = 1.3170731707317074 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 1.3 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row D-Allose: Km = 61.5 mM; kcat = 81 s-1; printed kcat/Km = 1.3 mM-1 s-1.

row_label: Table 1, printed substrate row D-Allose

status: verified


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row D-Ribose: column Km (mM) = 54.5; column kcat (s-1) = 49; column kcat/Km (mM-1 s-1) = 0.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 54.5 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 54.5 mM. kcat: printed Table 1 cell 49 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 49.0 s^(-1). kcat/Km: printed Table 1 cell 0.9 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 0.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 49 / 54.5 = 0.8990825688073395 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 0.9 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row D-Ribose: Km = 54.5 mM; kcat = 49 s-1; printed kcat/Km = 0.9 mM-1 s-1.

row_label: Table 1, printed substrate row D-Ribose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Fructose: column Km (mM) = 73.2; column kcat (s-1) = 116; column kcat/Km (mM-1 s-1) = 1.6.

normalized_value_unit_evidence: Km: printed Table 1 cell 73.2 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 73.2 mM. kcat: printed Table 1 cell 116 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 116.0 s^(-1). kcat/Km: printed Table 1 cell 1.6 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 1.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 116 / 73.2 = 1.5846994535519126 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 1.6 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Fructose: Km = 73.2 mM; kcat = 116 s-1; printed kcat/Km = 1.6 mM-1 s-1.


organism: Pseudomonas stutzeri

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329A to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329A block, row 'D-allose'; column 'Km (mM)' = 25.9; column 'Vmax (U/mg)' = 9.3; column 'kcat (s^-1)' = 7.4; column 'kcat/Km (mM^-1 s^-1)' = 2.8 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 25.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 25.9 mM. kcat: printed Table II cell 7.4 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 7.4 s^(-1). kcat/Km: printed Table II cell 2.8 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.28 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.28571428571428575.

raw_value_unit_evidence: Table II, S329A block, row D-allose: Km = 25.9 mM; kcat = 7.4 s^-1; printed kcat/Km = 2.8 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 9.3 U/mg.

row_label: Table II, S329A block, row D-allose

table_label: Table II: Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants (Protein Engineering, Design & Selection 2010, 23(12):919-927)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329F to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329F block, row 'D-allose'; column 'Km (mM)' = 53.3; column 'Vmax (U/mg)' = 4.7; column 'kcat (s^-1)' = 3.8; column 'kcat/Km (mM^-1 s^-1)' = 7.1 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 53.3 mM; the column head prints mM, so no unit conversion applies and the paper value is 53.3 mM. kcat: printed Table II cell 3.8 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 3.8 s^(-1). kcat/Km: printed Table II cell 7.1 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.071 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.07129455909943715.

raw_value_unit_evidence: Table II, S329F block, row D-allose: Km = 53.3 mM; kcat = 3.8 s^-1; printed kcat/Km = 7.1 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 4.7 U/mg.

row_label: Table II, S329F block, row D-allose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329K to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329K block, row 'D-allose'; column 'Km (mM)' = 33.9; column 'Vmax (U/mg)' = 3.4; column 'kcat (s^-1)' = 2.7; column 'kcat/Km (mM^-1 s^-1)' = 8.1 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 33.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 33.9 mM. kcat: printed Table II cell 2.7 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 2.7 s^(-1). kcat/Km: printed Table II cell 8.1 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.081 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.07964601769911506.

raw_value_unit_evidence: Table II, S329K block, row D-allose: Km = 33.9 mM; kcat = 2.7 s^-1; printed kcat/Km = 8.1 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 3.4 U/mg.

row_label: Table II, S329K block, row D-allose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329L to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329L block, row 'D-allose'; column 'Km (mM)' = 35.6; column 'Vmax (U/mg)' = 12.2; column 'kcat (s^-1)' = 9.8; column 'kcat/Km (mM^-1 s^-1)' = 2.7 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 35.6 mM; the column head prints mM, so no unit conversion applies and the paper value is 35.6 mM. kcat: printed Table II cell 9.8 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 9.8 s^(-1). kcat/Km: printed Table II cell 2.7 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.27 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.2752808988764045.

raw_value_unit_evidence: Table II, S329L block, row D-allose: Km = 35.6 mM; kcat = 9.8 s^-1; printed kcat/Km = 2.7 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 12.2 U/mg.

row_label: Table II, S329L block, row D-allose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), Wild-type block, row 'D-allose'; column 'Km (mM)' = 44.7; column 'Vmax (U/mg)' = 26.5; column 'kcat (s^-1)' = 21.2; column 'kcat/Km (mM^-1 s^-1)' = 4.7 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 44.7 mM; the column head prints mM, so no unit conversion applies and the paper value is 44.7 mM. kcat: printed Table II cell 21.2 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 21.2 s^(-1). kcat/Km: printed Table II cell 4.7 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.47 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.4742729306487695.

raw_value_unit_evidence: Table II, Wild-type block, row D-allose: Km = 44.7 mM; kcat = 21.2 s^-1; printed kcat/Km = 4.7 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 26.5 U/mg.

row_label: Table II, Wild-type block, row D-allose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329A block, row 'D-ribose'; column 'Km (mM)' = 44.4; column 'Vmax (U/mg)' = 11; column 'kcat (s^-1)' = 8.9; column 'kcat/Km (mM^-1 s^-1)' = 2.0 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 44.4 mM; the column head prints mM, so no unit conversion applies and the paper value is 44.4 mM. kcat: printed Table II cell 8.9 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 8.9 s^(-1). kcat/Km: printed Table II cell 2.0 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.2 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.20045045045045046.

raw_value_unit_evidence: Table II, S329A block, row D-ribose: Km = 44.4 mM; kcat = 8.9 s^-1; printed kcat/Km = 2.0 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 11 U/mg.

row_label: Table II, S329A block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329F block, row 'D-ribose'; column 'Km (mM)' = 39.1; column 'Vmax (U/mg)' = 2.1; column 'kcat (s^-1)' = 1.7; column 'kcat/Km (mM^-1 s^-1)' = 4.3 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 39.1 mM; the column head prints mM, so no unit conversion applies and the paper value is 39.1 mM. kcat: printed Table II cell 1.7 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 1.7 s^(-1). kcat/Km: printed Table II cell 4.3 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.043 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.043478260869565216.

raw_value_unit_evidence: Table II, S329F block, row D-ribose: Km = 39.1 mM; kcat = 1.7 s^-1; printed kcat/Km = 4.3 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 2.1 U/mg.

row_label: Table II, S329F block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329K block, row 'D-ribose'; column 'Km (mM)' = 67.3; column 'Vmax (U/mg)' = 2.3; column 'kcat (s^-1)' = 1.8; column 'kcat/Km (mM^-1 s^-1)' = 2.7 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 67.3 mM; the column head prints mM, so no unit conversion applies and the paper value is 67.3 mM. kcat: printed Table II cell 1.8 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 1.8 s^(-1). kcat/Km: printed Table II cell 2.7 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.027 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.026745913818722142.

raw_value_unit_evidence: Table II, S329K block, row D-ribose: Km = 67.3 mM; kcat = 1.8 s^-1; printed kcat/Km = 2.7 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 2.3 U/mg.

row_label: Table II, S329K block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329L block, row 'D-ribose'; column 'Km (mM)' = 65.6; column 'Vmax (U/mg)' = 4.1; column 'kcat (s^-1)' = 3.3; column 'kcat/Km (mM^-1 s^-1)' = 5.0 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 65.6 mM; the column head prints mM, so no unit conversion applies and the paper value is 65.6 mM. kcat: printed Table II cell 3.3 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 3.3 s^(-1). kcat/Km: printed Table II cell 5.0 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.05 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.05030487804878049.

raw_value_unit_evidence: Table II, S329L block, row D-ribose: Km = 65.6 mM; kcat = 3.3 s^-1; printed kcat/Km = 5.0 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 4.1 U/mg.

row_label: Table II, S329L block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), Wild-type block, row 'D-ribose'; column 'Km (mM)' = 85.1; column 'Vmax (U/mg)' = 14; column 'kcat (s^-1)' = 11.4; column 'kcat/Km (mM^-1 s^-1)' = 1.3 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 85.1 mM; the column head prints mM, so no unit conversion applies and the paper value is 85.1 mM. kcat: printed Table II cell 11.4 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 11.4 s^(-1). kcat/Km: printed Table II cell 1.3 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.13 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.1339600470035253.

raw_value_unit_evidence: Table II, Wild-type block, row D-ribose: Km = 85.1 mM; kcat = 11.4 s^-1; printed kcat/Km = 1.3 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 14 U/mg.

row_label: Table II, Wild-type block, row D-ribose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Lyxose: column Km (mM) = 33.4; column kcat (s-1) = 200; column kcat/Km (mM-1 s-1) = 6.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 33.4 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 33.4 mM. kcat: printed Table 1 cell 200 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 200.0 s^(-1). kcat/Km: printed Table 1 cell 6.0 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 6.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 200 / 33.4 = 5.9880239520958085 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 6.0 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Lyxose: Km = 33.4 mM; kcat = 200 s-1; printed kcat/Km = 6.0 mM-1 s-1.

row_label: Table 1, printed substrate row L-Lyxose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Mannose: column Km (mM) = 36.8; column kcat (s-1) = 155; column kcat/Km (mM-1 s-1) = 4.2.

normalized_value_unit_evidence: Km: printed Table 1 cell 36.8 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 36.8 mM. kcat: printed Table 1 cell 155 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 155.0 s^(-1). kcat/Km: printed Table 1 cell 4.2 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 4.2 s^(-1)*mM^(-1). Quotient disclosure for this row: 155 / 36.8 = 4.211956521739131 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 4.2 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Mannose: Km = 36.8 mM; kcat = 155 s-1; printed kcat/Km = 4.2 mM-1 s-1.


substrate_name: L-Xylulose

column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Xylulose: column Km (mM) = 63.0; column kcat (s-1) = 130; column kcat/Km (mM-1 s-1) = 2.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 63.0 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 63.0 mM. kcat: printed Table 1 cell 130 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 130.0 s^(-1). kcat/Km: printed Table 1 cell 2.1 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 2.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 130 / 63.0 = 2.0634920634920637 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 2.1 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Xylulose: Km = 63.0 mM; kcat = 130 s-1; printed kcat/Km = 2.1 mM-1 s-1.

substrate: L-Xylulose


substrate_name: L-Rhamnose

column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Rhamnose: column Km (mM) = 24.6; column kcat (s-1) = 195; column kcat/Km (mM-1 s-1) = 7.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 24.6 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 24.6 mM. kcat: printed Table 1 cell 195 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 195.0 s^(-1). kcat/Km: printed Table 1 cell 7.9 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 7.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 195 / 24.6 = 7.926829268292683 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 7.9 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Rhamnose: Km = 24.6 mM; kcat = 195 s-1; printed kcat/Km = 7.9 mM-1 s-1.

substrate: L-Rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329A to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329A with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=7.7 s^-1*mM^-1; package value 7.675675675675675 is consistent with displayed rounded table values.

row_label: S329A / Hexose / L-rhamnose

table_label: Table II Kinetic parameters of wild-type P. stutzeri L-RhI and Ser329 mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329F to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329F with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=0.55 s^-1*mM^-1; package value 0.5495867768595042 is consistent with displayed rounded table values.

row_label: S329F / Hexose / L-rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329K to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329K with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=0.41 s^-1*mM^-1; package value 0.4180327868852459 is consistent with displayed rounded table values.

row_label: S329K / Hexose / L-rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329L to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329L with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=6.8 s^-1*mM^-1; package value 6.784810126582278 is consistent with displayed rounded table values.

row_label: S329L / Hexose / L-rhamnose


column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for Wild-type with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=11.6 s^-1*mM^-1; package value 11.546391752577321 is consistent with displayed rounded table values.

row_label: Wild-type / Hexose / L-rhamnose


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D127N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D51N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H48A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R83N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T164A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


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

column_label: Table 1: Temperature Dependence of the Steady-State Kinetic Constants of eHisA and tHisA (Biochemistry 2002, 41(40):12032-12042); printed column heads enzyme | T (C) | kcat (s-1) | KMProFAR (uM) | kcat/KMProFAR (uM-1 s-1). Table 1, tHisA enzyme block, temperature row 37 C; column kcat (s-1) = 1.54; column KMProFAR (uM) = 0.6; column kcat/KMProFAR (uM-1 s-1) = 2.6. captured primary segment: tHisA | 37 | kcat 1.54 s^-1 | Km(ProFAR) 0.6 uM | kcat/Km(ProFAR) 2.6 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.54 s^-1; already in s^-1, no unit conversion applies; the exported value is 1.54 s^(-1). Km: printed Table 1 cell 0.6 uM; 1 uM is 1/1000 mM, so 0.6 / 1000 = 0.0006 mM; the exported value is 0.0006 mM. kcat/Km: printed Table 1 cell 2.6 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.6 x 1000 = 2600.0 s^-1 mM^-1. Quotient disclosure for this row: 1.54 / 0.0006 = 2566.666666666667 s^-1 mM^-1, which is the exported kcat_over_km, and 2566.666666666667 s^-1 mM^-1 is 2.566666666666667 uM^-1 s^-1, which the table prints to its own two figures as the cell 2.6.

raw_value_unit_evidence: Table 1, tHisA enzyme block, temperature row 37 C: kcat = 1.54 s^-1; Km(ProFAR) = 0.6 uM; printed kcat/Km(ProFAR) = 2.6 uM^-1 s^-1.


organism: Caldicellulosiruptor obsidiansis


substrate_name: D-allose

substrate: D-allose


substrate_name: L-rhamnose

substrate: L-rhamnose


organism: Caldicellulosiruptor saccharolyticus

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column D-allose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); D-allose: kcat 68.1 +/- 0.5 s^-1; KM 14.3 +/- 0.3 mM; kcat/KM 4.77 +/- 0.08 mM^-1 s^-1. Normalized without derivation to kcat=68.1 s^-1; Km=14.3 mM; kcat/Km=4.77 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / D-allose


normalized_value_unit_evidence: kcat normalized_value=78.7 normalized_unit=s^-1; Km normalized_value=3.64 normalized_unit=mM; computed kcat/Km normalized_value=21.62087912087912 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=78.7 (+/- 0.3) raw_unit=s^-1; Km raw_value=3.64 (+/- 0.08) raw_unit=mM; kcat/Km printed raw_value=21.6 (+/- 0.4) raw_unit=mM^-1 s^-1

row_label: C. saccharolyticus / l-mannose column

table_label: Table 4


column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column L-rhamnose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); L-rhamnose: kcat 99.9 +/- 2.4 s^-1; KM 1.03 +/- 0.20 mM; kcat/KM 97.1 +/- 17.3 mM^-1 s^-1. Normalized without derivation to kcat=99.9 s^-1; Km=1.03 mM; kcat/Km=97.1 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / L-rhamnose


column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column D-ribose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); D-ribose: kcat 118 +/- 2 s^-1; KM 33.5 +/- 1.3 mM; kcat/KM 3.54 +/- 0.09 mM^-1 s^-1. Normalized without derivation to kcat=118 s^-1; Km=33.5 mM; kcat/Km=3.54 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / D-ribose


column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column L-lyxose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); L-lyxose: kcat 186 +/- 3 s^-1; KM 3.65 +/- 0.25 mM; kcat/KM 50.8 +/- 2.7 mM^-1 s^-1. Normalized without derivation to kcat=186 s^-1; Km=3.65 mM; kcat/Km=50.8 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / L-lyxose


assay_conditions_summary: pH 7; 338.15 K; buffer 50 mM potassium phosphate

table_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively


column_label: Table 4; row group C. saccharolyticus (footnote a, this study); column l-mannose; sub-rows kcat (s^-1) = 78.7 +/- 0.3, KM (mM) = 3.64 +/- 0.08, kcat/KM (mM^-1 s^-1) = 21.6 +/- 0.4.

normalized_value_unit_evidence: kcat 78.7 s^-1 = 78.7 s^-1 (no conversion). Km 3.64 mM = 3.64 mM (no conversion). kcat/Km: the paper prints 21.6 mM^-1 s^-1 = 21.6 s^-1 mM^-1 (unit order only); the catalog holds the exact quotient of the paper's own cells, 78.7 / 3.64 = 21.62087912087912 s^-1 mM^-1, which rounds to the printed 21.6, so the only difference is printed precision.

raw_value_unit_evidence: Table 4, C. saccharolyticus row group, l-mannose column: kcat = 78.7 (+/- 0.3) s^-1; KM = 3.64 (+/- 0.08) mM; printed kcat/KM = 21.6 (+/- 0.4) mM^-1 s^-1.

row_label: C. saccharolyticus (this study), l-mannose column

table_label: Table 4. Comparison of Kinetic Parameters of the Recombinant l-RhIs ... for Isomerization of l-Rhamnose, l-Lyxose, l-Mannose, d-Allose, and d-Ribose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: L-gulose

substrate: L-gulose


organism: Thermoanaerobacterium saccharolyticum


substrate_name: D-ribose

substrate: D-ribose


column_label: Primary PMC HTML Table 2 row d-Mannose, column K_m (mM) = 34.0 +/- 1.1.

normalized_value_unit_evidence: Normalized paper Km: 34.0 mM, matching export Km 34.0 mM.

row_label: d-Mannose

table_label: Table 2. Kinetic parameters of recombinant CLLI


substrate_name: L-ribose

column_label: Primary PMC HTML Table 2 row l-Ribose, column K_m (mM) = 121.7 +/- 10.8.

normalized_value_unit_evidence: Normalized paper Km: 121.7 mM, matching export Km 121.7 mM.

row_label: l-Ribose

substrate: L-ribose


substrate_name: D-Lyxose

column_label: Table 2 row D-Lyxose lists Km 22.4 mM, kcat 1902 s^-1, and kcat/Km 84.9 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=22.4 normalized_unit=mM; kcat normalized_value=1902 normalized_unit=s^-1; kcat/Km normalized_value=84.9 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Km raw_value=22.4 raw_unit=mM; kcat raw_value=1902 raw_unit=s^-1; kcat/Km raw_value=84.9 raw_unit=mM^-1 s^-1

row_label: D-Lyxose

table_label: Table 2. Kinetic parameters of recombinant CLLI.

substrate: D-Lyxose


substrate_name: D-Mannose

column_label: Table 2 row D-Mannose lists Km 34.0 mM, kcat 46.1 s^-1, and kcat/Km 1.4 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=34.0 normalized_unit=mM; kcat normalized_value=46.1 normalized_unit=s^-1; kcat/Km normalized_value=1.4 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Km raw_value=34.0 raw_unit=mM; kcat raw_value=46.1 raw_unit=s^-1; kcat/Km raw_value=1.4 raw_unit=mM^-1 s^-1

row_label: D-Mannose

substrate: D-Mannose


substrate_name: L-Ribose

column_label: Table 2 row L-Ribose lists Km 121.7 mM, kcat 26.4 s^-1, and kcat/Km 0.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=121.7 normalized_unit=mM; kcat normalized_value=26.4 normalized_unit=s^-1; kcat/Km normalized_value=0.2 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Km raw_value=121.7 raw_unit=mM; kcat raw_value=26.4 raw_unit=s^-1; kcat/Km raw_value=0.2 raw_unit=mM^-1 s^-1

row_label: L-Ribose

substrate: L-Ribose


substrate_name: D-fructose

substrate: D-fructose


organism: Thermoclostridium stercorarium


substrate_name: D-allulose

substrate: D-allulose


organism: Medicago truncatula

substrate_name: PrFAR

proof_lines: kcat is 9.7 sec(-1) with PrFAR as substrate.

substrate: PrFAR


substrate_name: D-ribulose 5-phosphate

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

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

source_databases_merged: brenda skid

substrate: D-ribulose 5-phosphate


substrate_name: D-arabinose 5-phosphate

substrate: D-arabinose 5-phosphate


substrate_name: D-Arabinose 5-phosphate

substrate: D-Arabinose 5-phosphate


column_label: Table 1 (Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates) carries the columns Substrate | Product | Specific activity (umol min^-1 mg^-1) | Km (mmol l^-1) | kcat (s^-1) | kcat/Km ((mmol l^-1)^-1 s^-1), with the substrate rows grouped under the block labels Aldose, Ketose and Aldose phosphate. The cited cell set is the Ketose block, substrate row D-Fructose (product D-Mannose): Specific activity (umol min^-1 mg^-1) = 1.41; Km (mmol l^-1) = 19.4; kcat (s^-1) = 4297; kcat/Km ((mmol l^-1)^-1 s^-1) = 222.

normalized_value_unit_evidence: Km: printed Table 1 cell 19.4 under the column head Km (mmol l^-1); 1 mmol l^-1 is 1 mM, so no unit conversion applies and the paper value is 19.4 mM. kcat: printed Table 1 cell 4297 under the column head kcat (s^-1); the column is already in s^-1, so no unit conversion applies and the paper value is 4297.0 s^(-1). kcat/Km: printed Table 1 cell 222 under the column head kcat/Km ((mmol l^-1)^-1 s^-1); 1 (mmol l^-1)^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 222.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Ketose block, substrate row D-Fructose (product D-Mannose): Km = 19.4 mmol l^-1; kcat = 4297 s^-1; printed kcat/Km = 222 (mmol l^-1)^-1 s^-1.


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

substrate_name: D-galacturonate

proof_lines: kcat is 3.8 sec(-1) with D-galacturonate as substrate. kcat is 0.35 sec(-1) with D-glucuronate as substrate.

substrate: D-galacturonate


substrate_name: L-Ribulose

substrate: L-Ribulose


substrate_name: D-Xylulose

substrate: D-Xylulose


organism: Bacillus licheniformis

proof_lines: in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C


organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

substrate_name: Ru5P (at pH 7.8 and at 37 degrees Celsius)

column_label: Official PMC full text reports KpsF Km 0.30 +/- 0.03 mM for Ru5P and lists the same Ru5P Km in Table 2.

raw_value_unit_evidence: Km raw_value=0.30 +/- 0.03 raw_unit=mM for Ru5P.

row_label: recombinant KpsF / Ru5P

table_label: PMC1422761 full text kinetic parameters prose and Table 2


substrate_name: A5P (at pH 7.8 and at 37 degrees Celsius)


organism: Escherichia coli (strain K12)

substrate_name: Ru5P (at pH 8.25 and at 37 degrees Celsius)


substrate_name: A5P (at pH 8.25 and at 37 degrees Celsius)


organism: Clostridium tetani


substrate_name: Ru5P (at pH 8.5 and at 37 degrees Celsius)

column_label: Official JBC Results/Kinetic Parameters prose reports apparent Km for Ru5P as 0.35 +/- 0.08 mM.

raw_value_unit_evidence: Km raw_value=0.35 +/- 0.08 raw_unit=mM

table_label: Official JBC fulltext Results prose: Kinetic Parameters


substrate_name: A5P (at pH 8.5 and at 37 degrees Celsius)


substrate_name: L-rhamnose

substrate: L-rhamnose


substrate_name: L-rhamnulose

substrate: L-rhamnulose


organism: Arabidopsis thaliana

column_label: Abstract reports when D-arabinose-5-phosphate was used as substrate, Km and Vmax of AtKdsD values were 0.16 mmol/L and 0.18 mmol/L min.

raw_value_unit_evidence: Km raw_value=0.16 mmol/L raw_unit=mmol/L

row_label: Arabidopsis thaliana AtKdsD / D-arabinose-5-phosphate

table_label: PubMed XML abstract PMID 29022307


organism: Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)

substrate: A5P (at pH 8.5 and at 37 degrees Celsius)


organism: Francisella tularensis


organism: Cohnella laeviribosi

substrate_name: D-Lyxose


substrate_name: L-lyxose

substrate: L-lyxose


organism: Escherichia coli


organism: Serratia proteamaculans

substrate_name: D-fructose

normalized_value_unit_evidence: paper normalized kcat_over_km=222 s^-1*mM^-1; expected normalized value 221.49484536082477 s^-1*mM^-1 agrees by table rounding/SD

row_label: D-Fructose -> D-Mannose


column_label: PMC HTML Table 2 labeled Kinetic properties of YdaE_BL has D-Lyxose row with columns Km (mM)=30.4, kcat (s^-1)=98, and kcat/Km (mM^-1 s^-1)=3.2; exported central kcat/Km equals 98/30.4=3.223684210526316.

normalized_value_unit_evidence: Km normalized_value=30.4 normalized_unit=mM; kcat normalized_value=98 normalized_unit=s^-1; kcat_over_km normalized_value=3.223684210526316 normalized_unit=s^-1 mM^-1 from 98/30.4 central values.

raw_value_unit_evidence: PMC HTML Table 2 / prose: D-Lyxose row gives Km 30.4 mM, kcat 98 s^-1, and kcat/Km 3.2 mM^-1 s^-1.

row_label: D-Lyxose row for YdaE_BL

table_label: Table 2 / kinetic-parameters prose


substrate_name: D-Mannose

column_label: Official PMC Table 2, D-Mannose row: Km 26 +/- 0.8; kcat 43 +/- 0.1; kcat/Km 1.6.

normalized_value_unit_evidence: Km 26 mM; kcat 43 s^-1; independently printed kcat/Km 1.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 D-Mannose row: Km 26 +/- 0.8 mM; kcat 43 +/- 0.1 s^-1; independently printed kcat/Km 1.6 mM^-1 s^-1.

table_label: Table 2. Kinetic properties of YdaE BL


organism: Streptomyces coelicolor


substrate_name: D-glucuronate

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

substrate: D-glucuronate


organism: Thermofilum sp. (strain ex4484_79)

column_label: Biochemical characterization text states that TsLI is strictly dependent on divalent cations, showing highest activity with Mn2+ ions with a Km of 0.4 mM.

raw_value_unit_evidence: Km raw_value=0.4 mM raw_unit=mM

row_label: Thermofilum sp. D-lyxose isomerase / Mn2+ ion dependency

table_label: PMC full-text PMID 34422783 / Figure 3B divalent-cation kinetics text


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


substrate_name: D-ribose

assay_conditions_summary: pH 7; 338.15 K; buffer and 1 mM Co2+ at pH 7

proof_lines: at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0

substrate: D-ribose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: D-allose

substrate: D-allose


substrate_name: L-Lyxose

substrate: L-Lyxose


organism: Aeribacillus pallidus


proof_lines: at pH 7.5 and 40°C, in the presence of 1 mM Mn2+

substrate: D-fructose


substrate_name: D-mannose

substrate: D-mannose


substrate: D-Lyxose


substrate_name: D-xylulose

substrate: D-xylulose


organism: Providencia stuartii

assay_conditions_summary: pH 7.5; 318.15 K; buffer 50 mM HEPES


proof_lines:
in 50 mM HEPES buffer, at pH 7.5, 45°C
pH 6.5, 45°C


organism: Bacillus subtilis

substrate_name: L-arabinose

substrate: L-arabinose


organism: Halalkalibacterium halodurans

assay_conditions_summary: pH 7; 343.15 K; buffer 50 mM malate

proof_lines: in 50 mM malate buffer, at pH 7.0 and 70°C


organism: Dictyoglomus turgidum

substrate_name: L-ribulose

proof_lines:
at pH 7.5 and 75°C
pH 7.5, 75°C

substrate: L-ribulose


organism: Lactiplantibacillus plantarum

substrate_name: D-galactose

proof_lines:
pH 7.5, 60°C, recombinant enzyme
pH 7.0, 50°C, recombinant enzyme

substrate: D-galactose


organism: Bacillus velezensis

substrate_name: L-ribose

substrate: L-ribose


substrate_name: D-arabinose 5-phosphate

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

substrate: D-arabinose 5-phosphate


substrate_name: Unknown

substrate: Unknown


substrate_name: D-galacturonate

substrate: D-galacturonate


enzyme_display_name: UniProt O31662

enzyme: UniProt O31662


substrate_name: L-rhamnose

substrate: L-rhamnose


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: deuteroporphyrin IX

proof_lines: mutant E272S, in the presence of 4 mM Mg2+, pH 7.4, room temperature

enzyme: protoporphyrin ferrochelatase

substrate: deuteroporphyrin IX


enzyme_display_name: D-tagatose 3-epimerase

organism: Pseudomonas sp.

substrate_name: D-tagatose

enzyme: D-tagatose 3-epimerase

substrate: D-tagatose


proof_lines:
Co2+ substituted enzyme
Fe2+ substituted enzyme
pH 7.0, 22°C


enzyme_display_name: ribose isomerase

organism: Mycolicibacterium smegmatis

enzyme: ribose isomerase

substrate: D-ribose


organism: Klebsiella aerogenes

substrate_name: D-Lyxose


substrate_name: mannose

substrate: mannose


enzyme_display_name: cysteine-S-conjugate beta-lyase

substrate_name: cystathionine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: cystathionine


enzyme_display_name: phosphoribosylanthranilate isomerase

organism: Ogataea henricii

enzyme: phosphoribosylanthranilate isomerase


enzyme_display_name: corticosteroid side-chain-isomerase

organism: Mesocricetus auratus

enzyme: corticosteroid side-chain-isomerase


enzyme_display_name: L-fucose isomerase

organism: Caldanaerobius polysaccharolyticus

substrate_name: L-fucose

proof_lines:
pH 6.5, 55°C, recombinant enzyme
pH 6.5, 55°C

enzyme: L-fucose isomerase

substrate: L-fucose


enzyme_display_name: hydroxypyruvate isomerase

organism: Metabacillus fastidiosus

substrate_name: Hydroxypyruvate

enzyme: hydroxypyruvate isomerase

substrate: Hydroxypyruvate


organism: Thermotoga maritima

sequence_variant_note: Mutation signature D173V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Mutation signature D130V/D176V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D169V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Mutation signature D127V/D173V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127V/D169V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C


proof_lines: wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C


organism: Escherichia coli O45:K1 (strain S88 / ExPEC)

proof_lines: kcat is 0.49 sec(-1) with 5-methylthioribose-1-phosphate as substrate. kcat is 2.02 sec(-1) with 5-deoxyribose 1-phosphate as substrate. kcat is 0.67 sec(-1) with ribose-1-phosphate as substrate.


substrate_name: 5-deoxyribose 1-phosphate

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

substrate: 5-deoxyribose 1-phosphate


organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)

substrate_name: 5-deoxy-alpha-D-ribose 1-phosphate

proof_lines: kcat is 3.5 sec(-1) with 5-deoxy-alpha-D-ribose 1-phosphate as substrate.

substrate: 5-deoxy-alpha-D-ribose 1-phosphate


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

proof_lines: kcat is 0.1 sec(-1) with methylthioribose-1-phosphate as substrate. kcat is 0.18 sec(-1) with deoxyribose-1-phosphate as substrate (PubMed:23042035). kcat is 0.03 sec(-1) with ribose-1-phosphate as substrate (PubMed:31950558).


organism: Methanocaldococcus jannaschii

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


proof_lines: pH 7.0, 60°C, coupled assay, recombinant enzyme


organism: Caldicellulosiruptor saccharolyticus


organism: Bacillus subtilis (strain 168)

substrate_name: methylthioribose-1-phosphate (at pH 8.5 and 35 degrees Celsius)


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: ProFAR

substrate: ProFAR


organism: Thermanaeromonas toyohensis


organism: Escherichia coli (strain K12)

substrate_name: hydroxypyruvate (at 37 degrees Celsius and pH 7.0)


substrate_name: 5-deoxy-D-ribose 1-phosphate

substrate: 5-deoxy-D-ribose 1-phosphate


sequence_variant_note: Mutation signature D130T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 25°C, D130T, mutant form of imidazole glycerol phosphate synthase


proof_lines: kcat is 0.125 sec(-1) with L-xylulose as substrate.


organism: Dictyoglomus turgidum

substrate_name: L-Fucose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V131A to reconstruct the assayed variant sequence.

substrate: L-Fucose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W102A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W510A to reconstruct the assayed variant sequence.


organism: Klebsiella pneumoniae

proof_lines:
constitutive mutant 531
constitutive mutant 502


substrate_name: D-arabinose

substrate: D-arabinose


organism: Streptomyces coelicolor


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D373A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F452A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M197A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N404A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N538A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q314A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R30A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S405A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y451A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


enzyme_display_name: glutamate racemase

organism: Bacillus subtilis

substrate_name: D-glutamate

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

assay_conditions_summary: pH 8; buffer potassium phosphate

proof_lines: His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)

enzyme: glutamate racemase

substrate: D-glutamate


organism: Escherichia coli

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

proof_lines:
E. coli B/r
E. coli K-12


sequence_variant_note: Mutation signature D130V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 25°C, D130V, mutant form of imidazole glycerol phosphate synthase

proof_lines: mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C


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

proof_lines: pH 7.5, 25°C, D130P, mutant form of imidazole glycerol phosphate synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127G with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127G, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127K with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127K, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127F with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127F, mutant form of EC 5.3.1.6


sequence_variant_note: Mutation signature D127T matches the mutant residue at offset +0 and the reference residue at offset +22; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 7.5, 25°C, D127T, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127V, mutant form of EC 5.3.1.6

proof_lines: mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C


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

proof_lines: pH 7.5, 25°C, D127V/T164H, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R19A to reconstruct the assayed variant sequence.

proof_lines: PriA mutant R19A, PRA isomerase activity


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

proof_lines:
PriA, PRA isomerase activity
Raw SKiD Env: Temp=-----, pH=-----


organism: Raoultella sp.

substrate_name: L-Fuculose

substrate: L-Fuculose


substrate_name: D-ribulose

substrate: D-ribulose


enzyme_display_name: UniProt P63224

substrate_name: D-sedoheptulose 7-phosphate

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

enzyme: UniProt P63224

substrate: D-sedoheptulose 7-phosphate


enzyme_display_name: UniProt Q93UJ2

organism: Burkholderia pseudomallei

enzyme: UniProt Q93UJ2


enzyme_display_name: coproporphyrin ferrochelatase

substrate_name: coproporphyrin III

enzyme: coproporphyrin ferrochelatase

substrate: coproporphyrin III


substrate_name: L-xylulose

substrate: L-xylulose


organism: uncultured bacterium

substrate_name: D-arabino-hex-3-ulose 6-phosphate

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

substrate: D-arabino-hex-3-ulose 6-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: chorismate mutase

substrate_name: chorismate

proof_lines:
pH 7.5, 37°C, recombinant BsCM_2
pH 7.5, 37°C, recombinant AroH
strain WB672

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: sulfoquinovose isomerase

substrate_name: D-mannose

proof_lines: kcat is 79 sec(-1) for the formation of SF from SQ (PubMed:33791429). kcat is 25.3 sec(-1) for D-mannose. kcat is 22.2 sec(-1) for D-fructose. kcat is 13.5 sec(-1) for D-lyxose. kcat is 10.3 sec(-1) for D-xylulose (PubMed:18328504).

enzyme: sulfoquinovose isomerase

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-lyxose

substrate: D-lyxose


substrate_name: D-xylulose

substrate: D-xylulose


enzyme_display_name: D-sedoheptulose-7-phosphate isomerase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H61Q with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

enzyme: D-sedoheptulose-7-phosphate isomerase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R69Q to reconstruct the assayed variant sequence.


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

proof_lines: kcat is 23.3 sec(-1) for D-mannose. kcat is 12.3 sec(-1) for D-fructose.


organism: Geobacillus thermopakistaniensis


organism: Thermotoga maritima

proof_lines:
pH 7.5, 25°C, dimer
in 50 mM HEPES, pH 7.5 at 25°C
pH 7.5, 45°C, dimer


enzyme_display_name: amino-acid racemase

substrate_name: L-lysine

enzyme: amino-acid racemase

substrate: L-lysine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: Table 2 MtbGmhA wild-type row lists Km 0.31+/-0.06 mM in the Km (mM) column.

raw_value_unit_evidence: MtbGmhA wild-type row reports Km raw_value=0.31+/-0.06 raw_unit=mM.

row_label: MtbGmhA wild-type row

table_label: PMC7705670 Table 2


enzyme_display_name: galactose-6-phosphate isomerase

organism: Staphylococcus aureus

substrate_name: D-tagatose 6-phosphate

enzyme: galactose-6-phosphate isomerase

substrate: D-tagatose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D61A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H64Q to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt Q6T1W8

organism: Aneurinibacillus thermoaerophilus

enzyme: UniProt Q6T1W8


organism: Methylococcus capsulatus

substrate_name: D-arabino-3-hexulose 6-phosphate

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

substrate: D-arabino-3-hexulose 6-phosphate


column_label: Abstract states the apparent Michaelis constants for phospho-3-hexuloisomerase are D-arabino-3-hexulose 6-phosphate 1.0x10(-4) M and D-fructose 6-phosphate 1.1x10(-3) M.

raw_value_unit_evidence: Km raw_value=1.1x10(-3) raw_unit=M

row_label: Methylococcus capsulatus phospho-3-hexuloisomerase reverse reaction with D-fructose 6-phosphate

table_label: PubMed/PMC abstract PMID 4219834


enzyme_display_name: ribose-1,5-bisphosphate isomerase

organism: Thermococcus kodakarensis

substrate_name: alpha-D-ribose 1,5-bisphosphate

enzyme: ribose-1,5-bisphosphate isomerase

substrate: alpha-D-ribose 1,5-bisphosphate


enzyme_display_name: peptidylprolyl isomerase

substrate_name: RNase T1

enzyme: peptidylprolyl isomerase

substrate: RNase T1


organism: Mycobacterium tuberculosis

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


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

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


substrate_name: D-Homocysteinesulfinate

proof_lines: pH and temperature not specified in the publication

substrate: D-Homocysteinesulfinate


proof_lines: mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C


proof_lines: mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C


proof_lines: wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C


enzyme_display_name: phenylpyruvate tautomerase

organism: Mycolicibacterium smegmatis

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

assay_conditions_summary: pH 8; 295.15 K; buffer in 50 mM Tris-SO4

proof_lines: wild type enzyme CCH2, in in 50 mM Tris-SO4 buffer (pH 8.0), at 22°C

enzyme: phenylpyruvate tautomerase


assay_conditions_summary: pH 7.3; 295.15 K; buffer 10 mM Na2HPO4

proof_lines: wild type enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C

proof_lines: wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C

proof_lines: wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C


substrate_name: phenylenolpyruvate

proof_lines: mutant enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C

substrate: phenylenolpyruvate


organism: Streptomyces fradiae


organism: Pseudomonas pavonaceae

substrate_name: enol-phenylpyruvate

substrate: enol-phenylpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R15Y/H95R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R15Y/H95R, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R15Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H95R with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: Table 1: Kinetic Parameters and Sugar Product Analyses (Biochemistry 2015, 54(29):4495-4506), enzyme row 'FdtA wild-type'; column 'Km (mM)' = 0.50; column 'kcat (s-1)' = 10.5; column 'kcat/Km (M-1 s-1)' = 2.1 x 10^4; column '% original sugar epimer' = 100.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.50 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.5 mM; the exported value is 0.5 mM. kcat: printed Table 1 cell 10.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 10.5 s^(-1); the exported value is 10.5 s^(-1). kcat/Km: printed Table 1 cell 2.1 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21.0 s^-1 mM^-1; the exported value is 21.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'FdtA wild-type': Km = 0.50 mM; kcat = 10.5 s-1; printed kcat/Km = 2.1 x 10^4 M-1 s-1.

row_label: Table 1, enzyme row 'FdtA wild-type'


organism: Mus musculus

sequence_variant_note: Mutation signature E16A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: oxaloacetate tautomerase

organism: Arabidopsis thaliana

substrate_name: enol-oxaloacetate

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Table 1 row At FAHD2 lists OAA tautomerase (enol->keto) K_M 66.0 ± 4.9 uM, kcat 0.7 ± 0.1 s^-1, and kcat/K_M 1.10 × 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.066 normalized_unit=mM; kcat normalized_value=0.7 normalized_unit=s^-1; kcat/Km normalized_value=11.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=66.0 ± 4.9 raw_unit=uM; kcat raw_value=0.7 ± 0.1 raw_unit=s^-1; kcat/K_M raw_value=1.10 × 10^4 raw_unit=M^-1 s^-1

row_label: At FAHD2

table_label: Table 1. Kinetic properties of FAHD enzymes

enzyme: oxaloacetate tautomerase

substrate: enol-oxaloacetate


column_label: Table 1 row At FAHD1 lists OAA tautomerase (enol->keto) K_M 48.8 ± 1.8 uM, kcat 3.7 ± 0.5 s^-1, and kcat/K_M 7.48 × 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0488 normalized_unit=mM; kcat normalized_value=3.7 normalized_unit=s^-1; kcat/Km normalized_value=74.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=48.8 ± 1.8 raw_unit=uM; kcat raw_value=3.7 ± 0.5 raw_unit=s^-1; kcat/K_M raw_value=7.48 × 10^4 raw_unit=M^-1 s^-1

row_label: At FAHD1


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: D-sedoheptulose 7-phosphate (at 30 degrees Celsius)

proof_lines: kcat is 0.14 sec(-1) for D-sedoheptulose 7-phosphate.


organism: Homo sapiens

column_label: Table 1 row Hs FAHD1 lists OAA tautomerase (enol->keto) K_M 15.8 ± 5.9 uM, kcat 31.1 ± 4.5 s^-1, and kcat/K_M 1.99 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0158 normalized_unit=mM; kcat normalized_value=31.1 normalized_unit=s^-1; kcat/Km normalized_value=1990 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=15.8 ± 5.9 raw_unit=uM; kcat raw_value=31.1 ± 4.5 raw_unit=s^-1; kcat/K_M raw_value=1.99 × 10^6 raw_unit=M^-1 s^-1

row_label: Hs FAHD1


column_label: Table 1 row Hs FAHD2B lists OAA tautomerase (enol->keto) K_M 296 ± 12 uM, kcat 68.7 ± 3.3 s^-1, and kcat/K_M 2.32 × 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.296 normalized_unit=mM; kcat normalized_value=68.7 normalized_unit=s^-1; kcat/Km normalized_value=232 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=296 ± 12 raw_unit=uM; kcat raw_value=68.7 ± 3.3 raw_unit=s^-1; kcat/K_M raw_value=2.32 × 10^5 raw_unit=M^-1 s^-1

row_label: Hs FAHD2B


column_label: Table 1 row Hs FAHD2A lists OAA tautomerase (enol->keto) K_M 22.2 ± 3.6 uM, kcat 13.6 ± 2.8 s^-1, and kcat/K_M 6.28 × 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0222 normalized_unit=mM; kcat normalized_value=13.6 normalized_unit=s^-1; kcat/Km normalized_value=628 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=22.2 ± 3.6 raw_unit=uM; kcat raw_value=13.6 ± 2.8 raw_unit=s^-1; kcat/K_M raw_value=6.28 × 10^5 raw_unit=M^-1 s^-1

row_label: Hs FAHD2A


organism: Escherichia coli (strain K12)

substrate_name: fumarate

proof_lines: kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.

substrate: fumarate


proof_lines: kcat is 29.2 sec(-1) (in the presence of AMP, at 85 degrees Celsius).

source_databases_merged: brenda skid uniprot


substrate_name: sulfoquinovose

column_label: Primary article text states EcYihS exhibited Michaelis-Menten parameters for formation of SF from SQ with KM = 1.89 +/- 0.28 mM, referenced to Figure S2.

raw_value_unit_evidence: Km raw_value=1.89 +/- 0.28 raw_unit=mM

row_label: EcYihS-catalyzed formation of SF from SQ

table_label: Results text and Figure S2, SQ isomerase YihS kinetics

substrate: sulfoquinovose


organism: Bos taurus

column_label: Table 1 row Bt FAHD2A lists OAA tautomerase (enol->keto) K_M 20.2 ± 1.4 uM, kcat 32.7 ± 3.0 s^-1, and kcat/K_M 1.63 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0202 normalized_unit=mM; kcat normalized_value=32.7 normalized_unit=s^-1; kcat/Km normalized_value=1630 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=20.2 ± 1.4 raw_unit=uM; kcat raw_value=32.7 ± 3.0 raw_unit=s^-1; kcat/K_M raw_value=1.63 × 10^6 raw_unit=M^-1 s^-1

row_label: Bt FAHD2A


organism: Bacillus subtilis


substrate_name: keto-(p-hydroxyphenyl)pyruvate

proof_lines:
23°C, pH 6.5
Raw SKiD Env: Temp=23°C, pH=6.5
Raw SKiD Env: Temp=23°C, pH=-----

substrate: keto-(p-hydroxyphenyl)pyruvate


substrate_name: enol-(p-hydroxyphenyl)pyruvate

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.

substrate: enol-(p-hydroxyphenyl)pyruvate


sequence_variant_note: Mutation signature P1G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
23°C, mutant enzyme P1G
23°C, pH 6.5, mutant enzyme P1G


sequence_variant_note: Mutation signature N97A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Trichinella spiralis

substrate_name: Unknown

substrate: Unknown


proof_lines: kcat is 3.7 sec(-1) with enol-oxaloacetate as substrate.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K32A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K32R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y95F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y97A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines: kcat is 31.1 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 13.6 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 210 nmol/min/mg for the decarboxylation of oxaloacetate. kcat is 140 nmol/min/mg for the hydrolysis of acetylpyruvate.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 369 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 0.7 sec(-1) with enol-oxaloacetate as substrate.


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 237 sec(-1) with enol-oxaloacetate as substrate (PubMed:38287013). kcat is 0.52 sec(-1) with oxaloacetate as substrate for koxaloacetate decarboxylase activity (PubMed:38287013).


proof_lines: kcat is 32.7 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 161 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 68.7 sec(-1) with enol-oxaloacetate as substrate.


organism: Aneurinibacillus thermoaerophilus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H95R with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R15Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R15Y/H95R to reconstruct the assayed variant sequence.


table_label: Table 1: Kinetic Parameters and Sugar Product Analyses (Biochemistry 2015, 54(29):4495-4506)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y35F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines:
23°C, pH 6.5, wild-type enzyme
23°C, wild-type enzyme


column_label: Table 1 row Sc FMP41 lists OAA tautomerase (enol->keto) K_M 219 ± 23 uM, kcat 369 ± 41 s^-1, and kcat/K_M 1.75 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.219 normalized_unit=mM; kcat normalized_value=369 normalized_unit=s^-1; kcat/Km normalized_value=1750 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=219 ± 23 raw_unit=uM; kcat raw_value=369 ± 41 raw_unit=s^-1; kcat/K_M raw_value=1.75 × 10^6 raw_unit=M^-1 s^-1

row_label: Sc FMP41


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: acetylpyruvate

substrate: acetylpyruvate


substrate_name: oxaloacetate (with oxaloacetate decarboxylase activity)


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: D-tartrate

substrate: D-tartrate


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


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


column_label: Table 1 row Bs YisK lists OAA tautomerase (enol->keto) K_M 43.8 ± 8.1 uM, kcat 237 ± 8 s^-1, and kcat/K_M 5.81 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0438 normalized_unit=mM; kcat normalized_value=237 normalized_unit=s^-1; kcat/Km normalized_value=5810 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=43.8 ± 8.1 raw_unit=uM; kcat raw_value=237 ± 8 raw_unit=s^-1; kcat/K_M raw_value=5.81 × 10^6 raw_unit=M^-1 s^-1

row_label: Bs YisK


substrate_name: keto-oxaloacetate

proof_lines:
enzyme form OAT-1, 25°C, pH 9.0
enzyme form OAT-1

substrate: keto-oxaloacetate


proof_lines:
enzyme form OAT-2, 25°C, pH 9.0
enzyme form OAT-1, 25°C, pH 9.0
enzyme form OAT-1


substrate_name: keto-phenylpyruvate

column_label: Table 3; substrate row 1; columns Km, kcat, and kcat/Km

normalized_value_unit_evidence: normalized: Km=4.9 mM; kcat=285 s^-1; kcat/Km=58 s^-1 mM^-1

raw_value_unit_evidence: paper Table 3 cells for substrate 1: Km=4900 (1000) uM; kcat=285 (40) s^-1; kcat/Km=5.8 x 10^4 M^-1 s^-1

row_label: substrate 1 / keto phenylpyruvate

table_label: Table 3

substrate: keto-phenylpyruvate


substrate_name: (S)-malate

proof_lines: kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.

substrate: (S)-malate


organism: Sus scrofa

proof_lines:
enol-form, kidney
keto-form, kidney
thyroid gland


proof_lines:
keto-form, kidney
thyroid gland


enzyme_display_name: L-arabinose isomerase

organism: Bacillus velezensis

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


enzyme_display_name: cellobiose epimerase

organism: Bacteroides fragilis

substrate_name: cellobiose

proof_lines: recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C

proof_lines: pH and temperature not specified in the publication

enzyme: cellobiose epimerase

substrate: cellobiose


enzyme_display_name: UDP-glucose 4-epimerase

organism: Bifidobacterium bifidum

substrate_name: UDPgalactose

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: adenylate cyclase

organism: Bombyx mori

enzyme: adenylate cyclase


organism: Bordetella pertussis

proof_lines:
in the presence of Mn2+
in 75 mM HEPES/NaOH, pH 7.4, at 25°C
in the presence of Mg2+


substrate_name: ATP

assay_conditions_summary: cofactor ATP

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

proof_lines: pH and temperature not specified in the publication, in presence of calmodulin

substrate: ATP


enzyme_display_name: aspartate racemase

substrate_name: D-Asp

enzyme: aspartate racemase

substrate: D-Asp