assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

column_label: Official PLOS PDF text extraction lines 564-578: Table 1; row TIM1WT; columns Km (mM), Kcat(min^-1), Kcat/Km (mM^-1 min^-1); cells 0.23 +/- 0.02, 7.98 X 10^4, 3.5 X 10^5.

raw_value_unit_evidence: Table 1 TIM1WT row reports Km 0.23 mM, Kcat 7.98 X 10^4 min^-1, and Kcat/Km 3.5 X 10^5 mM^-1 min^-1.

table_label: Table 1. Catalytic parameters of ball and socket TvTIM mutants


enzyme_display_name: triose-phosphate isomerase

organism: Saccharomyces cerevisiae

substrate_name: dihydroxyacetone 3-phosphate

source_db: brenda

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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

km_unit: mM

sequence_source: multiple

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

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

proof_lines:
at pH 7.5 and 37°C
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.4

data_origin: experimental

source_databases_merged: brenda skid

enzyme: triose-phosphate isomerase

substrate: dihydroxyacetone 3-phosphate

source: brenda


organism: Gemmata obscuriglobus

substrate_name: D-Glyceraldehyde 3-phosphate

source_db: oed

source_license: CC BY 4.0

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

substrate: D-Glyceraldehyde 3-phosphate

source: oed


organism: Gallus gallus


organism: Homo sapiens

substrate_name: D-glyceraldehyde 3-phosphate (at pH 7.4 and 25 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

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

mutation_type: substitution

source: uniprot


organism: Trichomonas vaginalis

substrate_name: D-glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V45A to reconstruct the assayed variant sequence.

substrate: D-glyceraldehyde 3-phosphate


organism: Trypanosoma brucei brucei

substrate_name: glycerone phosphate

verification_status: unverified

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

substrate: glycerone phosphate

status: unverified


organism: Streptomyces coelicolor


organism: Trypanosoma brucei

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


proof_lines:
mutant enzymeR191A
mutant enzyme R191A


organism: Giardia duodenalis


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


organism: Helicobacter pylori


proof_lines: mutant I170T, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant I170V, pH not specified in the publication, temperature not specified in the publication


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


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Plasmodium falciparum

proof_lines: mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C


proof_lines: mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C


proof_lines: mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C


proof_lines: mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C


proof_lines: mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C


proof_lines:
pH 7.4, 25°C, mutant enzyme C14S
mutant C14S, 25°C, pH 7.4


proof_lines:
wild-type enzyme
wild-type, 25°C, pH 7.6
wild-type, pH 7.6, 25°C


organism: Saccharolobus solfataricus

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


organism: Arabidopsis thaliana


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V167P/W168E to reconstruct the assayed variant sequence.


substrate_name: dihydroxyacetone phosphate

assay_conditions_summary: pH 7.5; 298.15 K; buffer 30 mM triethanolamine

proof_lines: mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C

substrate: dihydroxyacetone phosphate


proof_lines: wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C


proof_lines: mutant F96A, 25°C, pH not specified in the publication


proof_lines: mutant F96S/L167V, 25°C, pH not specified in the publication


proof_lines: mutant F96S/S73A, 25°C, pH not specified in the publication


proof_lines: mutant F96Y, 25°C, pH not specified in the publication


proof_lines: mutant F96S, 25°C, pH not specified in the publication


proof_lines: above, pH 7.6, mutants F96W, F96S, and F96H


proof_lines: mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C


proof_lines: in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C

proof_lines: in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C


proof_lines: in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C

proof_lines: in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C


proof_lines:
monomeric mutant A178L, pH 7.6, 25°C
mutant A178L, pH 7.6, 25°C


proof_lines:
monomeric wild-type, pH 7.6, 25°C
wild-type, 25°C, pH 7.6
wild-type, pH 7.6, 25°C


proof_lines:
monomeric wild-type, pH 7.6, 25°C
wild-type, 25°C, pH 7.6
wild-type, 25°C, pH 7.4


organism: Trypanosoma cruzi

proof_lines: mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C


proof_lines: mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C

proof_lines: mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C


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


organism: Leishmania mexicana

proof_lines:
glycerone phosphate
recombinant enzyme


proof_lines: mutant enzyme C13D, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication


proof_lines: mutant enzyme C13E, in 100 mM triethanolamine-HCl (pH 7.6), temperature not specified in the publication


assay_conditions_summary: pH 7.6; 298.15 K; buffer TEA

proof_lines: mutant enzyme E97Q, in TEA buffer (pH 7.6, 100 mM), at 25°C


proof_lines: mutant enzyme E165A, in TEA buffer (pH 7.6, 100 mM), at 25°C


enzyme_display_name: peptidylprolyl isomerase

organism: Thermus thermophilus

substrate_name: TRYWNAKMK-(cis)-PFIFGA

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

enzyme: peptidylprolyl isomerase

substrate: TRYWNAKMK-(cis)-PFIFGA


proof_lines: mutant lacking the insert-in-flap domain, pH 7.5, temperature not specified in the publication


organism: Moritella marina

proof_lines:
wild type enzyme
pH 7.6, wild-type enzyme
wild-type enzyme


proof_lines: wild type enzyme, in 100 mM TEA (pH 7.5), at 25°C

proof_lines: wild type enzyme, at pH 7.5 (30 mM triethanolamine), 25°C

proof_lines: wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C


organism: Equus caballus


enzyme_display_name: phosphomannomutase

organism: Acinetobacter haemolyticus

substrate_name: alpha-D-mannose 1-phosphate

enzyme: phosphomannomutase

substrate: alpha-D-mannose 1-phosphate


organism: Escherichia coli

proof_lines: mutant enzyme G148D, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C


proof_lines: mutant enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C


proof_lines: wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C

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


organism: Acetivibrio thermocellus


enzyme_display_name: alanine racemase

organism: Aeromonas hydrophila subsp. hydrophila

proof_lines: pH 11.0, 35°C, recombinant His-tagged enzyme

enzyme: alanine racemase


organism: Trypanosoma brucei brucei

proof_lines: mutant enzyme L232A, at pH 7.5 (30 mM triethanolamine), 25°C


enzyme_display_name: UDP-glucose 4-epimerase

organism: Aeromonas hydrophila

substrate_name: UDP-galactose

enzyme: UDP-glucose 4-epimerase

substrate: UDP-galactose


enzyme_display_name: maleate isomerase

organism: Alcaligenes faecalis

substrate_name: Maleate

enzyme: maleate isomerase

substrate: Maleate


organism: Secale cereale

proof_lines:
cytosolic enzyme
chloroplastic enzyme


proof_lines:
glycerone phosphate, cytosolic enzyme
chloroplastic enzyme


enzyme_display_name: chorismate mutase

organism: Amborella trichopoda

substrate_name: chorismate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, recombinant enzyme

enzyme: chorismate mutase

substrate: chorismate


organism: Alkalihalophilus pseudofirmus

substrate_name: D-alanine / L-alanine

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

substrate: D-alanine / L-alanine


enzyme_display_name: cysteine-S-conjugate beta-lyase

substrate_name: L-cystine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystine


substrate_name: UDP-glucose / UDP-D-galactose / UDP-galactose

proof_lines: The approximate value is estimated from reaction velocities at saturating substrate concentrations (5?9 mM).

proof_lines: Different enzyme concentrations give slight variations in activity.


enzyme_display_name: isochorismate synthase

enzyme: isochorismate synthase


substrate_name: D-alanine

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

substrate: D-alanine


proof_lines: recombinant enzyme, pH 8.0, temperature not specified in the publication


organism: Oryctolagus cuniculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Δ208 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: 20°C, pH 7.4, mutant DELTA208-213, presence of 1 mM MgATP


proof_lines: 20°C, pH 7.4, wild-type, presence of 1 mM MgATP


organism: Arabidopsis thaliana


enzyme_display_name: UDP-arabinose 4-epimerase

substrate_name: UDP-D-xylose

proof_lines: recombinant Arabidopsis thaliana enzyme, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)

proof_lines: recombinant Arabidopsis thaliana enzyme UGE2, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)

enzyme: UDP-arabinose 4-epimerase

substrate: UDP-D-xylose


substrate_name: D-mannose 1-phosphate

substrate: D-mannose 1-phosphate


enzyme_display_name: phosphoacetylglucosamine mutase

substrate_name: alpha-D-glucose 1-phosphate

enzyme: phosphoacetylglucosamine mutase

substrate: alpha-D-glucose 1-phosphate


enzyme_display_name: magnesium dechelatase

substrate_name: chlorophyllin a

enzyme: magnesium dechelatase

substrate: chlorophyllin a


enzyme_display_name: UniProt Q2VMT2

organism: Alicyclobacillus acidocaldarius

substrate_name: L-arabinose

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=65°C, pH=6
Raw SKiD Env: Temp=65°C, pH=7
Raw SKiD Env: Temp=65°C, pH=8

enzyme: UniProt Q2VMT2

substrate: L-arabinose

source: skid


enzyme_display_name: UniProt D9ILD9

organism: Limosilactobacillus fermentum

substrate_name: D-galactose

proof_lines:
Raw SKiD Env: Temp=65°C, pH=6
Raw SKiD Env: Temp=65°C, pH=6.5
Raw SKiD Env: Temp=65°C, pH=5

enzyme: UniProt D9ILD9

substrate: D-galactose


enzyme_display_name: UniProt Q5KYP7

organism: Geobacillus kaustophilus

enzyme: UniProt Q5KYP7


enzyme_display_name: L-arabinose isomerase

organism: Thermoanaerobacterium saccharolyticum

enzyme: L-arabinose isomerase


enzyme_display_name: UniProt P12851

organism: Actinoplanes missouriensis

substrate_name: D-glucose

enzyme: UniProt P12851

substrate: D-glucose


substrate_name: L-ribose

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

substrate: L-ribose


enzyme_display_name: UniProt P26997

organism: Thermus thermophilus

substrate_name: D-xylose

enzyme: UniProt P26997

substrate: D-xylose


substrate_name: D-mannose

substrate: D-mannose


enzyme_display_name: xylose isomerase

substrate_name: D-Xylose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N91D to reconstruct the assayed variant sequence.

enzyme: xylose isomerase

substrate: D-Xylose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N91D/V144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N91D/D375G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N91D/D375G/V385A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N91D/K355A to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt O50083

organism: Pyrococcus horikoshii

substrate_name: D-ribulose 5-phosphate

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

enzyme: UniProt O50083

substrate: D-ribulose 5-phosphate


substrate_name: D-ribose 5-phosphate

proof_lines:
Raw SKiD Env: Temp=93°C, pH=6
Raw SKiD Env: Temp=50°C, pH=6

substrate: D-ribose 5-phosphate


enzyme_display_name: UniProt Q4CQE2

organism: Trypanosoma cruzi

substrate_name: D-Ribose 5-diphosphate

enzyme: UniProt Q4CQE2

substrate: D-Ribose 5-diphosphate


enzyme_display_name: UniProt Q9X0G9

organism: Thermotoga maritima

substrate_name: D-ribose

enzyme: UniProt Q9X0G9

substrate: D-ribose


substrate_name: D-allose

substrate: D-allose


substrate_name: L-talose

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

substrate: L-talose


enzyme_display_name: mannose isomerase

organism: Thermosediminibacter oceani

substrate_name: D-fructose

enzyme: mannose isomerase

substrate: D-fructose


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: D-Mannose

substrate: D-Mannose


enzyme_display_name: UniProt P34948

organism: Candida albicans

substrate_name: D-mannose 6-phosphate

enzyme: UniProt P34948

substrate: D-mannose 6-phosphate


enzyme_display_name: glucose-6-phosphate isomerase

organism: Schistosoma mansoni

substrate_name: fructose 6-phosphate

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

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


organism: Dictyostelium discoideum


organism: Apis mellifera

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Thermococcus kodakarensis

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt P06744

organism: Homo sapiens

substrate_name: D-glucose 6-phosphate

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

proof_lines:
Raw SKiD Env: Temp=21°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.5

enzyme: UniProt P06744

substrate: D-glucose 6-phosphate


organism: Arabidopsis thaliana

substrate_name: L-cystine

substrate: L-cystine


enzyme_display_name: alanine racemase

organism: Alkalihalophilus pseudofirmus

substrate_name: D-alanine

proof_lines: pH 10.5, 40°C, recombinant wild-type enzyme

enzyme: alanine racemase

substrate: D-alanine


enzyme_display_name: tRNA-intron lyase

organism: Archaeoglobus fulgidus

substrate_name: pretRNA

proof_lines: wild-type protein, substrate: 5'-AAGCGACCGACC*AUA*GCUGCA-3' or 5'-AAUGCAGCGGUC*AAA*GGUCGC-3'

enzyme: tRNA-intron lyase

substrate: pretRNA


enzyme_display_name: aldose 1-epimerase

organism: Aspergillus niger

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: triose-phosphate isomerase

organism: Plasmodium falciparum

substrate_name: D-glyceraldehyde 3-phosphate

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


assay_conditions_summary: pH 7.6; 296.15 K; buffer TEA

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

proof_lines: wild type enzyme, in TEA buffer (pH 7.6, 100 mM), at 25°C


enzyme_display_name: guanylate cyclase

organism: Arbacia punctulata

substrate_name: GTP

enzyme: guanylate cyclase

substrate: GTP


enzyme_display_name: D-cysteine desulfhydrase

substrate_name: D-cysteine

sequence_source: UniProt F4HYF3

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

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-Ribose 5-diphosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-Ribose 5-diphosphate


substrate_name: D-ribulose 5-diphosphate

substrate: D-ribulose 5-diphosphate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: D-arabinose isomerase

organism: Thermanaeromonas toyohensis

substrate_name: D-altrose

enzyme: D-arabinose isomerase

substrate: D-altrose


substrate_name: L-fucose

substrate: L-fucose


substrate_name: D-arabinose

substrate: D-arabinose


organism: Thermus aquaticus

substrate_name: D-xylose

proof_lines: D-ribose D-glucose

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-xylulose

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

substrate: D-xylulose


enzyme_display_name: L-arabinose isomerase

organism: Alicyclobacillus hesperidum

substrate_name: D-galactose

enzyme: L-arabinose isomerase

substrate: D-galactose


substrate_name: L-Arabinose

substrate: L-Arabinose


organism: Klebsiella pneumoniae

proof_lines:
constitutive mutant 531
constitutive mutant 502


organism: Thermotoga maritima

substrate_name: D-allose

substrate: D-allose


substrate_name: D-ribose

proof_lines:
pH 8.0 and 70°C
pH 8.0, 70°C

substrate: D-ribose


substrate_name: L-talose

substrate: L-talose


organism: Geobacillus stearothermophilus

substrate_name: D-Fructose 6-phosphate

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

substrate: D-Fructose 6-phosphate


organism: Caballeronia jiangsuensis

substrate_name: D-Lyxose

proof_lines: recombinant His-tagged enzyme, pH 7.0, 55°C

substrate: D-Lyxose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


organism: Deltaproteobacteria bacterium


sequence_variant_note: Resolved canonical sequence from uniprot_accession_inactive_uniparc and applied mutation signature D478K with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_inactive_uniparc and applied mutation signature D478N with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_inactive_uniparc and applied mutation signature D478Q with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


organism: Clostridioides difficile


substrate_name: D-Ribose 5-phosphate

substrate: D-Ribose 5-phosphate


organism: Lactobacillus gayonii

substrate_name: L-ribulose

substrate: L-ribulose


substrate_name: L-arabinose

substrate: L-arabinose


enzyme_display_name: xylose isomerase

organism: Opuntia ficus-indica

proof_lines: enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C

enzyme: xylose isomerase


organism: Stenotrophomonas rhizophila

proof_lines: pH 7.0, 50°C, recombinant wild-type enzyme


organism: Streptomyces flavogriseus

proof_lines:
soluble enzyme
immobilized enzyme


organism: Streptomyces viridobrunneus

substrate_name: xylose

substrate: xylose


substrate_name: glucose

substrate: glucose


organism: Trypanosoma cruzi

substrate_name: D-ribulose 5-phosphate

proof_lines: in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C

substrate: D-ribulose 5-phosphate


substrate_name: D-allose 6-phosphate

substrate: D-allose 6-phosphate


organism: Caldicellulosiruptor saccharolyticus

substrate_name: D-altrose

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

substrate: D-altrose


substrate_name: D-arabinose

substrate: D-arabinose


organism: Pseudomonas syringae


organism: Opuntia vulgaris

substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


organism: Bos taurus

substrate_name: fructose 6-phosphate

proof_lines:
mammary gland enzyme
isozyme 1 and isozyme 2
fructose 6-phosphate, isozyme 4

substrate: fructose 6-phosphate


substrate_name: glucose 6-phosphate

proof_lines: mammary gland enzyme, values of 0.12 mM and 0.57 mM are determined by different authors

substrate: glucose 6-phosphate


organism: Cassia coluteoides

substrate_name: D-fructose 6-phosphate

proof_lines:
isoenzyme PGI I from germinating seeds
isoenzyme PGI II from developing seeds
isoenzyme PGI II from germinating seeds

substrate: D-fructose 6-phosphate


substrate_name: D-glucose 6-phosphate

proof_lines:
isoenzyme PGI II from germinating seeds
isoenzyme PGI I from germinating seeds
isoenzyme PGI II from developing seeds

substrate: D-glucose 6-phosphate


organism: Pseudothermotoga lettingae

substrate_name: D-psicose

substrate: D-psicose


organism: Lentzea aerocolonigenes

substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


organism: Spinacia oleracea

proof_lines:
isozyme 1 and 2
chloroplastic isoenzyme


proof_lines: fructose 6-phosphate, cytosolic isoenzame

proof_lines: glucose 6-phosphate, cytosolic and chloroplastic isoenzyme


organism: Agrobacterium tumefaciens


organism: Mycolicibacterium smegmatis


organism: Pseudomonas savastanoi pv. phaseolicola


enzyme_display_name: mannose-6-phosphate isomerase

organism: Amorphophallus konjac

substrate_name: mannose 6-phosphate

enzyme: mannose-6-phosphate isomerase

substrate: mannose 6-phosphate


organism: Gluconobacter thailandicus


proof_lines:
enzyme from developing seeds
enzyme from germinating seeds


organism: Thermotoga maritima

substrate_name: D-ribose 5-phosphate

proof_lines:
at 60°C and pH 7.0
at 80°C and pH 7.0
pH 8.0 and 70°C

substrate: D-ribose 5-phosphate


organism: Dehalococcoides mccartyi

substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Acetivibrio thermocellus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R132K with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R132I with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R132Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


verification_status: verified

assay_conditions_summary: pH 7.5; 353.15 K; buffer 50 mM Tris-HCl

column_label: Table 2, enzyme row Wild type; column Specific activity (nmol min-1 mg-1) = 1,994; column Km (mM) = 53; column kcat (s-1) = 2,347; column kcat/Km (mM-1 s-1) = 44.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2,347 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 2347.0 s^(-1). Km: printed Table 2 cell 53 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 53.0 mM. kcat/Km: printed Table 2 cell 44 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 44.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Wild type: Specific activity = 1,994 nmol min-1 mg-1; Km = 53 mM; kcat = 2,347 s-1; printed kcat/Km = 44 mM-1 s-1.

row_label: Table 2, enzyme row Wild type

table_label: Table 2: Kinetic parameters and specific activities of the wild-type and mutant enzymes at position 132 of ribose-5-phosphate isomerases from C. thermocellum for D-psicose (Appl Microbiol Biotechnol 2011, 89:1859-1866)

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R132A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R132D with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R132E with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


organism: Burkholderia cenocepacia

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


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


organism: Pyrococcus horikoshii

substrate_name: beta-D-mannose 6-phosphate

substrate: beta-D-mannose 6-phosphate


organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R472A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R479A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R373A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E410A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E458A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N433A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H411A to reconstruct the assayed variant sequence.


organism: Geobacillus stearothermophilus

substrate_name: L-arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E261L to reconstruct the assayed variant sequence.

substrate: L-arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D118V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D195V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D333V to reconstruct the assayed variant sequence.


organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)

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

proof_lines: kcat is 315 sec(-1) with glucose 6-phosphate as substrate. kcat is 240 sec(-1) with mannose 6-phosphate as substrate. kcat is 265 sec(-1) with fructose 6-phosphate as substrate.


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L487F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L339P with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R472H with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


organism: Acidothermus cellulolyticus


substrate_name: D-galactose

substrate: D-galactose


substrate_name: beta-D-fructose 6-phosphate

proof_lines: pH 7.0, 22°C, recombinant wild-type enzyme

substrate: beta-D-fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H310A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q415A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K422A to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: L-fucose

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

source_databases_merged: brenda uniprot

substrate: L-fucose


substrate_name: D-arabinose

substrate: D-arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H18T with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: without borate, pH 8.0, 60°C, recombinant mutant H18T


organism: Piromyces sp.

substrate_name: D-xylose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E129D/V433I/E15D/E114G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer 100 mM Tris-HCl

proof_lines: mutant enzyme E129D/V433I/E15D/E114G, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C

substrate: D-xylose


sequence_variant_note: Mutation signature E129D/V433I/E15D/E114G/T142S/A177T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme E129D/V433I/E15D/E114G/T142S/A177T, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


organism: Thermotoga neapolitana

substrate_name: D-glucose

assay_conditions_summary: pH 7

proof_lines: soluble wild type enzyme, at 80°C, pH 7.0

proof_lines: soluble wild type enzyme, at 90°C, pH 7.0

substrate: D-glucose


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

proof_lines: unbound CBD-TNX fusion protein, at 80°C, pH 7.0

proof_lines: immobilized CBD-TNX fusion protein, at 80°C, pH 7.0

proof_lines: immobilized CBD-TNX fusion protein, at 90°C, pH 7.0


organism: Latilactobacillus sakei subsp. sakei


organism: Marinomonas mediterranea

substrate_name: D-talose

proof_lines: recombinant His-tagged enzyme, pH 7.4, 30°C

proof_lines: kcat is 329 sec(-1) with D-mannose as substrate. kcat is 64.4 sec(-1) with D-lyxose as substrate. kcat is 0.319 sec(-1) with D-talose as substrate.

substrate: D-talose


substrate_name: D-Lyxose

substrate: D-Lyxose


organism: Thermoanaerobacter mathranii


organism: Escherichia coli (strain K12)

substrate_name: L-xylulose

substrate: L-xylulose


organism: Pseudomonas cannabina pv. alisalensis

substrate_name: mannose

proof_lines: kcat is 0.766 sec(-1) with mannose as substrate. kcat is 0.581 sec(-1) with fructose as substrate.

substrate: mannose


substrate_name: fructose

substrate: fructose


organism: Thermotoga maritima

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

proof_lines: in the presence of 0.6 mM Mn2+, at pH 7.5 and 60°C

proof_lines: in the presence of 0.2 mM Mn2+, at pH 7.5 and 60°C


organism: Leishmania donovani

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A3Q8ID81 and applied mutation signature H138N to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'H138N'; column 'Km (mM)' = 8.14; column 'kcat (s-1)' = 11; column 'kcat / Km (M-1 s-1)' = 1355.07. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.364.

normalized_value_unit_evidence: kcat: printed Table 1 cell 11 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 11.0 s^(-1). Km: printed Table 1 cell 8.14 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 8.14 mM. kcat/Km: printed Table 1 cell 1355.07 in a column headed kcat / Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1355.07 / 1000 = 1.35507 s^-1 mM^-1. Before this pass the live export row carried kcat 11.0 s^(-1), Km 8.14 mM and kcat_over_km 1.3513513513513513 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'H138N': Km = 8.14 mM; kcat = 11 s-1; printed kcat/Km = 1355.07 in a column headed kcat / Km (M-1 s-1).

row_label: Table 1, row H138N

table_label: Table 1: Kinetic parameters for wild type LdRpiB and its mutants (PLoS ONE 2016, volume 11, issue 3, article e0150764). Printed column heads, in printed order: the unheaded enzyme-form column; Km (mM); Vmax (Umg-1min-1); kcat (s-1); kcat / Km (M-1 s-1).

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A3Q8ID81 and applied mutation signature P47A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'P47A'; column 'Km (mM)' = 4.30; column 'kcat (s-1)' = 18; column 'kcat / Km (M-1 s-1)' = 4241.06. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.294.

normalized_value_unit_evidence: kcat: printed Table 1 cell 18 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 18.0 s^(-1). Km: printed Table 1 cell 4.30 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 4.3 mM. kcat/Km: printed Table 1 cell 4241.06 in a column headed kcat / Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4241.06 / 1000 = 4.24106 s^-1 mM^-1. Before this pass the live export row carried kcat 18.0 s^(-1), Km 4.3 mM and kcat_over_km 4.186046511627907 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'P47A': Km = 4.30 mM; kcat = 18 s-1; printed kcat/Km = 4241.06 in a column headed kcat / Km (M-1 s-1).

row_label: Table 1, row P47A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A3Q8ID81 and applied mutation signature Y46F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'Y46F'; column 'Km (mM)' = 2.59; column 'kcat (s-1)' = 25; column 'kcat / Km (M-1 s-1)' = 9820.05. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.401.

normalized_value_unit_evidence: kcat: printed Table 1 cell 25 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 25.0 s^(-1). Km: printed Table 1 cell 2.59 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.59 mM. kcat/Km: printed Table 1 cell 9820.05 in a column headed kcat / Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9820.05 / 1000 = 9.82005 s^-1 mM^-1. Before this pass the live export row carried kcat 25.0 s^(-1), Km 2.59 mM and kcat_over_km 9.652509652509654 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'Y46F': Km = 2.59 mM; kcat = 25 s-1; printed kcat/Km = 9820.05 in a column headed kcat / Km (M-1 s-1).

row_label: Table 1, row Y46F


column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'RpiB (Wt)'; column 'Km (mM)' = 2.51; column 'kcat (s-1)' = 29; column 'kcat / Km (M-1 s-1)' = 11175.48. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.423.

normalized_value_unit_evidence: kcat: printed Table 1 cell 29 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 29.0 s^(-1). Km: printed Table 1 cell 2.51 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.51 mM. kcat/Km: printed Table 1 cell 11175.48 in a column headed kcat / Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11175.48 / 1000 = 11.17548 s^-1 mM^-1. Before this pass the live export row carried kcat 29.0 s^(-1), Km 2.51 mM and kcat_over_km 11.55378486055777 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'RpiB (Wt)': Km = 2.51 mM; kcat = 29 s-1; printed kcat/Km = 11175.48 in a column headed kcat / Km (M-1 s-1).

row_label: Table 1, row RpiB (Wt)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A3Q8ID81 and applied mutation signature H11N to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'H11N'; column 'Km (mM)' = 3.40; column 'kcat (s-1)' = 32; column 'kcat / Km (M-1 s-1)' = 9512.02. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.257.

normalized_value_unit_evidence: kcat: printed Table 1 cell 32 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 32.0 s^(-1). Km: printed Table 1 cell 3.40 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 3.4 mM. kcat/Km: printed Table 1 cell 9512.02 in a column headed kcat / Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9512.02 / 1000 = 9.512020000000001 s^-1 mM^-1. Before this pass the live export row carried kcat 32.0 s^(-1), Km 3.4 mM and kcat_over_km 9.411764705882353 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'H11N': Km = 3.40 mM; kcat = 32 s-1; printed kcat/Km = 9512.02 in a column headed kcat / Km (M-1 s-1).

row_label: Table 1, row H11N


organism: Spinacia oleracea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D87A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K100A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D90A with inferred residue-numbering offset -6 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.

proof_lines:
pH 7.5, 90°C
pH 7.0-7.5, 90°C, recombinant enzyme


column_label: Preparation and characterization prose reports K_m 3.1 +/- 0.2 mM for E. coli RpiA using ribose-5-phosphate.

raw_value_unit_evidence: Km raw_value=3.1 +/- 0.2 raw_unit=mM

row_label: E. coli RpiA / ribose-5-phosphate conversion assay

table_label: PMC full text PMID 12517338 RpiA preparation and characterization prose


organism: Mycobacterium tuberculosis

proof_lines: kcat is 120 sec(-1) for D-ribose 5-phosphate.

source_databases_merged: skid uniprot


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D85N to reconstruct the assayed variant sequence.


substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K125A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R100A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D168N to reconstruct the assayed variant sequence.


proof_lines:
50°C, pH 6.0, wild-type enzyme
93°C, pH 6, wild-type enzyme


organism: Thermosediminibacter oceani

substrate_name: D-fructose

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.

substrate: D-fructose


substrate_name: D-mannose

substrate: D-mannose


organism: Limosilactobacillus reuteri subsp. rodentium


organism: Thermoanaerobacterium saccharolyticum

assay_conditions_summary: pH 7.5; 343.15 K; buffer 25 mM Tris-HCl

proof_lines: in 25 mM Tris-HCl buffer (pH 7.5), at 60°C


organism: Homo sapiens

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q388A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 294.15 K; buffer 20 mM HEPES

proof_lines: mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)

substrate: D-glucose 6-phosphate


organism: Escherichia coli

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

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: Oryctolagus cuniculus

proof_lines: kcat is 0.0434 sec(-1) with mannose-6-phosphate as substrate.


organism: Thermobifida fusca

proof_lines: kcat is 788 sec(-1) with D-mannose as substrate. kcat is 63.3 sec(-1) with D-lyxose as substrate.


substrate_name: D-lyxose

substrate: D-lyxose


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

substrate_name: ribose 5-P

substrate: ribose 5-P


organism: Trypanosoma cruzi

substrate_name: D-ribulose 5-diphosphate

substrate: D-ribulose 5-diphosphate


organism: Acetivibrio thermocellus

proof_lines: avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C

proof_lines: avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C


organism: Pyrococcus furiosus

substrate_name: D-fructose 6-phosphate

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

substrate: D-fructose 6-phosphate


proof_lines:
50°C, pH 7.0, native enzyme
pH 7.0, 50°C
50°C, pH 7.0, recombinant enzyme


organism: Pseudoalteromonas haloplanktis

substrate_name: L-arabinose

proof_lines:
pH 7.0, 40°C
pH 8.0, 40°C, recombinant enzyme
pH 7.5, 75°C, recombinant enzyme

substrate: L-arabinose


organism: Escherichia coli (strain K12)

substrate_name: Unknown

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

substrate: Unknown


organism: Geobacillus stearothermophilus


substrate_name: D-ribose 5-phosphate

assay_conditions_summary: pH 7.5; 338.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer (pH 7.5), at 65°C

substrate: D-ribose 5-phosphate


assay_conditions_summary: pH 7.5; buffer 50 mM Tris-HCl


substrate_name: L-allose

substrate: L-allose


substrate_name: D-ribose

substrate: D-ribose


proof_lines: pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate

proof_lines: pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate


organism: Thermotoga maritima

substrate_name: D-Ribose 5-phosphate

substrate: D-Ribose 5-phosphate


organism: Escherichia coli O157:H7


organism: Pseudomonas cannabina pv. alisalensis

proof_lines: kcat is 0.766 sec(-1) with mannose as substrate. kcat is 0.581 sec(-1) with fructose as substrate.


organism: Serratia proteamaculans

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.


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.

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)

substrate: 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 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.


organism: Aeropyrum pernix


organism: Arabidopsis thaliana


organism: Bacillus subtilis

substrate_name: D-Talose

substrate: D-Talose


organism: Escherichia coli

proof_lines: kcat is 2100 sec(-1) for ribose-5-phosphate.


organism: Alicyclobacillus acidocaldarius

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K269E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines:
mutant K269E at pH 6 and 65°C
mutant K269E at pH 8 and 65°C
mutant K269E at pH 7 and 65°C


substrate_name: L-Ribose

substrate: L-Ribose


organism: Geobacillus thermodenitrificans

substrate_name: D-mannose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W17Q/N90A/L129F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C

substrate: D-mannose 6-phosphate


substrate_name: D-Mannose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L129F with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

substrate: D-Mannose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L129F with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature N90A/L129F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme N90A/L129F, at pH 7.0 and 70°C


organism: Thermoplasma acidophilum


organism: Methanocaldococcus jannaschii


organism: Mycobacterium tuberculosis


organism: Pyrobaculum aerophilum


organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)

proof_lines: kcat is 315 sec(-1) with glucose 6-phosphate as substrate. kcat is 240 sec(-1) with mannose 6-phosphate as substrate. kcat is 265 sec(-1) with fructose 6-phosphate as substrate.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N90A/L129F to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W17Q/N90A/L129F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: ribose-5-phosphate (at 50 degrees Celsius)

proof_lines: kcat is 1072 sec(-1) for ribose-5-phosphate.


organism: Pyrococcus furiosus

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


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae

substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


substrate_name: D-mannose

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.

substrate: D-mannose


organism: Archaeoglobus fulgidus

sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature Y95F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 343.15 K; cofactor NADP+

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row Y95F; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); Y95F: app. kcat 0.22 +/- 0.02 s^-1; app. Km(F6P) 0.36 +/- 0.05 mM; kcat/Km 0.61 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.22 s^-1; Km=0.36 mM; kcat/Km=0.61 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature Y95K to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row Y95K; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); Y95K: app. kcat 0.68 +/- 0.04 s^-1; app. Km(F6P) 0.18 +/- 0.08 mM; kcat/Km 3.8 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.68 s^-1; Km=0.18 mM; kcat/Km=3.8 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature E93D to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row E93D; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); E93D: app. kcat 0.06 +/- 0.01 s^-1; app. Km(F6P) 2.9 +/- 1.2 mM; kcat/Km 0.02 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.06 s^-1; Km=2.9 mM; kcat/Km=0.02 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature G79A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row G79A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); G79A: app. kcat 0.32 +/- 0.04 s^-1; app. Km(F6P) 0.5 +/- 0.1 mM; kcat/Km 0.64 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.32 s^-1; Km=0.5 mM; kcat/Km=0.64 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature G79L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row G79L; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); G79L: app. kcat 0.07 +/- 0.02 s^-1; app. Km(F6P) 2.0 +/- 0.2 mM; kcat/Km 0.035 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.07 s^-1; Km=2.0 mM; kcat/Km=0.035 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H136A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H136A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H136A: app. kcat 30.8 +/- 1.5 s^-1; app. Km(F6P) 0.19 +/- 0.04 mM; kcat/Km 162 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=30.8 s^-1; Km=0.19 mM; kcat/Km=162 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H80A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H80A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H80A: app. kcat 0.43 +/- 0.07 s^-1; app. Km(F6P) 20.3 +/- 5.3 mM; kcat/Km 0.02 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.43 s^-1; Km=20.3 mM; kcat/Km=0.02 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H80D to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H80D; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H80D: app. kcat 0.42 +/- 0.06 s^-1; app. Km(F6P) 0.39 +/- 0.05 mM; kcat/Km 1.1 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.42 s^-1; Km=0.39 mM; kcat/Km=1.1 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H82A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H82A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H82A: app. kcat 8.0 +/- 1.0 s^-1; app. Km(F6P) 2.0 +/- 0.2 mM; kcat/Km 4.0 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=8.0 s^-1; Km=2.0 mM; kcat/Km=4.0 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature T63A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row T63A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); T63A: app. kcat 1.9 +/- 0.1 s^-1; app. Km(F6P) 0.22 +/- 0.04 mM; kcat/Km 8.6 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=1.9 s^-1; Km=0.22 mM; kcat/Km=8.6 s^-1*mM^-1.


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

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row WT; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); WT: app. kcat 32.4 +/- 1.9 s^-1; app. Km(F6P) 0.25 +/- 0.05 mM; kcat/Km 130 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=32.4 s^-1; Km=0.25 mM; kcat/Km=130 s^-1*mM^-1.

row_label: WT


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row Y160F; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); Y160F: app. kcat 11.6 +/- 1.0 s^-1; app. Km(F6P) 1.4 +/- 0.4 mM; kcat/Km 8.3 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=11.6 s^-1; Km=1.4 mM; kcat/Km=8.3 s^-1*mM^-1.


organism: Serratia proteamaculans

substrate_name: D-fructose

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.

substrate: D-fructose


organism: Geobacillus stearothermophilus

substrate_name: D-Glucose 6-phosphate

substrate: D-Glucose 6-phosphate


organism: Homo sapiens

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y341F to reconstruct the assayed variant sequence.

substrate: D-glucose 6-phosphate


organism: Thermus thermophilus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H50A 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 Q48A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W13A 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 E132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E67A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H122A to reconstruct the assayed variant sequence.


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

substrate_name: fructose 6-phosphate

proof_lines: kcat is 17.4 sec(-1) with fructose 6-phosphate as substrate.

substrate: fructose 6-phosphate


organism: Bacillus coagulans

substrate_name: alpha-D-Fructofuranose

substrate: alpha-D-Fructofuranose


substrate_name: alpha-D-Glucose

substrate: alpha-D-Glucose


substrate_name: alpha-D-Xylose

substrate: alpha-D-Xylose


substrate_name: D-Fructose

substrate: D-Fructose


substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: D-Xylose

substrate: D-Xylose


substrate_name: D-Xylulose

assay_conditions_summary: pH 7; 308.15 K; buffer this record. Assay condition: 0.028 M Veronal/acetate

column_label: Table 1 (PDF page 5 of 8, journal page 289), substrate row `D-Xylulose`, enzyme source `B. coagulans`, Mn2+ columns: kcat Mn2+ (s^-1) = 11; Km Mn2+ (mM) = 0.40; kcat/Km Mn2+ (s^-1 M^-1) = 27500.

normalized_value_unit_evidence: kcat: printed cell 11 s^-1 is already the export unit s^(-1); the exported value is 11.0 s^(-1). Km: printed cell 0.40 mM is already the export unit mM; the exported value is 0.4 mM. kcat/Km: the paper PRINTS the kcat/Km cell 27500 s^-1 M^-1 for this line and 1 s^-1 M^-1 equals 0.001 s^(-1)*mM^(-1), so the printed cell is 27.5 s^(-1)*mM^(-1); the exported value is 27.5 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `D-Xylulose`, enzyme source `B. coagulans`

table_label: Table 1 (PDF page 5 of 8, journal page 289) 'Kinetic parameters for D-xylose and D-xylulose'

substrate: D-Xylulose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D511N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E495Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H100L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H396L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N154Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q388A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S185A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y274F to reconstruct the assayed variant sequence.


organism: Escherichia coli O157:H7

substrate_name: L-gulose

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

substrate: L-gulose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E372G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E372G/F163L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E372G/V379A to reconstruct the assayed variant sequence.


organism: Lactococcus lactis subsp. lactis


organism: Acetivibrio thermocellus

substrate_name: D-Psicose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

substrate: D-Psicose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132D with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132E with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132I with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132K with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


column_label: Table 2, enzyme row Wild type; column Specific activity (nmol min-1 mg-1) = 1,994; column Km (mM) = 53; column kcat (s-1) = 2,347; column kcat/Km (mM-1 s-1) = 44.


organism: Lactobacillus brevis


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K144A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K294A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K356A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R207K to reconstruct the assayed variant sequence.


substrate_name: L-Arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D308A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

substrate: L-Arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9S467 and applied mutation signature E351A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters determined for US100 L-AIs (wild type and mutants) (J. Bacteriol. 2007, 189(9):3556-3563), enzyme row 'E351A mutant'; column 'Km (mM)' = 30.1 ± 0.09; column 'kcat (min^-1)' = 174.3 ± 0.01; column 'kcat/Km (mM^-1 min^-1)' = 5.79; column 'Activity loss (%)' = 85.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 30.1 mM and the export unit is mM, so no unit conversion applies; the exported value is 30.1 mM. kcat: the printed Table 2 cell is 174.3 min^-1; min^-1 becomes s^-1 on division by 60, so 174.3 / 60 = 2.905 s^-1, which is the exported value 2.905 s^(-1). kcat/Km: the printed Table 2 cell is 5.79 mM^-1 min^-1, which converts as 5.79 / 60 = 0.0965 s^-1 mM^-1. The exported catalytic efficiency 0.09651162790697673 s^(-1)*mM^(-1) is the full-precision quotient 2.905 / 30.1 of those same two printed cells, and the paper's printed efficiency cell is that same quotient carried to the paper's own two-decimal place: 174.3 / 30.1 = 5.790698 mM^-1 min^-1, which the paper prints as 5.79.

raw_value_unit_evidence: Table 2, enzyme row 'E351A mutant': Km = 30.1 ± 0.09 mM; kcat = 174.3 ± 0.01 min^-1; printed kcat/Km = 5.79 mM^-1 min^-1; activity loss = 85 %.

row_label: Table 2, enzyme row 'E351A mutant'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F279Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9S467 and applied mutation signature H446A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters determined for US100 L-AIs (wild type and mutants) (J. Bacteriol. 2007, 189(9):3556-3563), enzyme row 'H446A mutant'; column 'Km (mM)' = 30.4 ± 0.28; column 'kcat (min^-1)' = 857.7 ± 0.12; column 'kcat/Km (mM^-1 min^-1)' = 28.21; column 'Activity loss (%)' = 57.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 30.4 mM and the export unit is mM, so no unit conversion applies; the exported value is 30.4 mM. kcat: the printed Table 2 cell is 857.7 min^-1; min^-1 becomes s^-1 on division by 60, so 857.7 / 60 = 14.295 s^-1, which is the exported value 14.295 s^(-1). kcat/Km: the printed Table 2 cell is 28.21 mM^-1 min^-1, which converts as 28.21 / 60 = 0.4701666666666667 s^-1 mM^-1. The exported catalytic efficiency 0.47023026315789473 s^(-1)*mM^(-1) is the full-precision quotient 14.295 / 30.4 of those same two printed cells, and the paper's printed efficiency cell is that same quotient carried to the paper's own two-decimal place: 857.7 / 30.4 = 28.213816 mM^-1 min^-1, which the paper prints as 28.21.

raw_value_unit_evidence: Table 2, enzyme row 'H446A mutant': Km = 30.4 ± 0.28 mM; kcat = 857.7 ± 0.12 min^-1; printed kcat/Km = 28.21 mM^-1 min^-1; activity loss = 57 %.

row_label: Table 2, enzyme row 'H446A mutant'


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

column_label: Table 2: Kinetic parameters determined for US100 L-AIs (wild type and mutants) (J. Bacteriol. 2007, 189(9):3556-3563), enzyme row 'WT'; column 'Km (mM)' = 28.42 ± 0.12; column 'kcat (min^-1)' = 2036.4 ± 0.07; column 'kcat/Km (mM^-1 min^-1)' = 71.65; column 'Activity loss (%)' = 0.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 28.42 mM and the export unit is mM, so no unit conversion applies; the exported value is 28.42 mM. kcat: the printed Table 2 cell is 2036.4 min^-1; min^-1 becomes s^-1 on division by 60, so 2036.4 / 60 = 33.94 s^-1, which is the exported value 33.94 s^(-1). kcat/Km: the printed Table 2 cell is 71.65 mM^-1 min^-1, which converts as 71.65 / 60 = 1.1941666666666668 s^-1 mM^-1. The exported catalytic efficiency 1.1942294159042925 s^(-1)*mM^(-1) is the full-precision quotient 33.94 / 28.42 of those same two printed cells, and the paper's printed efficiency cell is that same quotient carried to the paper's own two-decimal place: 2036.4 / 28.42 = 71.653765 mM^-1 min^-1, which the paper prints as 71.65.

raw_value_unit_evidence: Table 2, enzyme row 'WT': Km = 28.42 ± 0.12 mM; kcat = 2036.4 ± 0.07 min^-1; printed kcat/Km = 71.65 mM^-1 min^-1; activity loss = 0 %.

row_label: Table 2, enzyme row 'WT' (the wild-type US100 L-AI)


substrate_name: L-Fucose

substrate: L-Fucose


organism: Thermococcus litoralis

substrate_name: D-Fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E98V to reconstruct the assayed variant sequence.

substrate: D-Fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H137A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H89A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H91A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


organism: Streptomyces violaceoruber

sequence: GVTFHDDDLIPF

wild_type_sequence: GVTFHDDDLIPF


substrate_name: L-ribulose

substrate: L-ribulose


substrate_name: D-talose

substrate: D-talose


substrate_name: L-ribose

substrate: L-ribose


substrate_name: L-tagatose

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

substrate: L-tagatose


substrate_name: D-psicose

substrate: D-psicose


organism: Arthrobacter sp.


substrate_name: D-Lyxose

column_label: Table 3; row D-Lyxose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row D-Lyxose (30 deg C): Km=86 mM; Vmax=0.086 umol/min per mg; kcat=3.7 min^-1; kcat/Km=0.04 min^-1 mM^-1.

row_label: D-Lyxose (30 deg C)

table_label: Table 3. Kinetic parameters for purified Arthrobacter B3728 D-xylose isomerase

substrate: D-Lyxose


substrate_name: D-Ribose

column_label: Table 3; row D-Ribose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row D-Ribose (30 deg C): Km=190 mM; Vmax=0.71 umol/min per mg; kcat=30.9 min^-1; kcat/Km=0.16 min^-1 mM^-1.

row_label: D-Ribose (30 deg C)

substrate: D-Ribose


column_label: Table 3; row D-Xylose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row D-Xylose (30 deg C): Km=3.3 mM; Vmax=12.25 umol/min per mg; kcat=533 min^-1; kcat/Km=162 min^-1 mM^-1.

row_label: D-Xylose (30 deg C)


column_label: Table 3; row L-Arabinose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row L-Arabinose (30 deg C): Km=280 mM; Vmax=1.8 umol/min per mg; kcat=78.3 min^-1; kcat/Km=0.28 min^-1 mM^-1.

row_label: L-Arabinose (30 deg C)


organism: Leishmania donovani

substrate_name: D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession:G9JM00 and applied mutation signature H11N to reconstruct the assayed variant sequence.

column_label: PMID 26953696, PDF page 7 / 20, Table 1, row H11N, columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1).

normalized_value_unit_evidence: Same-row central values: Km 3.40 mM; kcat 32 s^-1; independently printed kcat/Km 9.51202 s^-1 mM^-1 after dividing the M^-1 value by 1000.

table_label: Table 1

substrate: D-Ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession:G9JM00 and applied mutation signature H138N to reconstruct the assayed variant sequence.

column_label: PMID 26953696, PDF page 7 / 20, Table 1, row H138N, columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1).

normalized_value_unit_evidence: Same-row central values: Km 8.14 mM; kcat 11 s^-1; independently printed kcat/Km 1.35507 s^-1 mM^-1 after dividing the M^-1 value by 1000.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:G9JM00 and applied mutation signature P47A to reconstruct the assayed variant sequence.

column_label: PMID 26953696, PDF page 7 / 20, Table 1, row P47A, columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1).

normalized_value_unit_evidence: Same-row central values: Km 4.30 mM; kcat 18 s^-1; independently printed kcat/Km 4.24106 s^-1 mM^-1 after dividing the M^-1 value by 1000.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G9JM00 and applied mutation signature Y46F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'Y46F'; column 'Km (mM)' = 2.59; column 'kcat (s-1)' = 25; column 'kcat / Km (M-1 s-1)' = 9820.05. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.401.


column_label: PMID 26953696, PDF page 7 / 20, Table 1, row RpiB (Wt), columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1); footnote ND, not determined.

normalized_value_unit_evidence: Same-row central values: Km 2.51 mM; kcat 29 s^-1; independently printed kcat/Km 11.17548 s^-1 mM^-1 after dividing the M^-1 value by 1000.

row_label: RpiB (Wt)


organism: Actinoplanes missouriensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F26W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q256D with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D256R to reconstruct the assayed variant sequence.


substrate_name: D-Mannose

substrate: D-Mannose


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

substrate_name: D-mannose 6-phosphate

column_label: Abstract reports apparent Km for D-mannose 6-phosphate was 3.03 mM.

raw_value_unit_evidence: Km raw_value=3.03 mM raw_unit=mM

row_label: Pseudomonas aeruginosa PMI-GMP / D-mannose 6-phosphate

table_label: PubMed XML abstract PMID 1846611

substrate: D-mannose 6-phosphate


substrate_name: D-mannose 1-phosphate

substrate: D-mannose 1-phosphate


substrate_name: GTP

substrate: GTP


substrate_name: GDP-D-mannose

substrate: GDP-D-mannose


organism: Spinacia oleracea

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E91A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

substrate_name: D-allose

substrate: D-allose


substrate_name: D-ribose

substrate: D-ribose


substrate_name: L-talose

substrate: L-talose


organism: Bacillus licheniformis

substrate_name: L-Arabinose

substrate: L-Arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: D-fructose

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

column_label: PubMed abstract reports the D-fructose row with Km 203.7 mM, kcat 27.7 s^-1, and catalytic efficiency 136.0 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=203.7 normalized_unit=mM; kcat normalized_value=27.7 normalized_unit=s^-1; kcat/Km normalized_value=0.136 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: D-fructose kinetic row: Km=203.7+/-6.7 mM; kcat=27.7+/-0.7 s^-1; catalytic efficiency=136.0+/-2.9 M^-1 s^-1

row_label: recombinant Escherichia coli BL21 d-mannose isomerase with d-fructose

table_label: PubMed abstract PMID 27138861

substrate: D-fructose


protein_accession_database: NCBI Protein


organism: Bacillus subtilis

column_label: Table 2 row D-Lyxose lists Km 433 +/- 3 mM, kcat 7089 +/- 78 s^-1, and kcat/Km 16.4 +/- 0.1 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=433 mM; kcat normalized=7089 s^-1; kcat/Km normalized=16.371824480369515 s^-1 mM^-1 from same-row quotient

row_label: D-Lyxose

table_label: Table 2. Kinetic parameters of B. subtilis mannose 6-phosphate isomerase for aldoses


column_label: Table 2 row D-Ribose lists Km 110 +/- 1 mM, kcat 72 +/- 1 s^-1, and kcat/Km 0.6 +/- 0.01 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=110 mM; kcat normalized=72 s^-1; kcat/Km normalized=0.6545454545454545 s^-1 mM^-1 from same-row quotient

row_label: D-Ribose


substrate_name: L-allose

column_label: Table 2 row L-Allose lists Km 312 +/- 14 mM, kcat 920 +/- 41 s^-1, and kcat/Km 2.9 +/- 0.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=312 mM; kcat normalized=920 s^-1; kcat/Km normalized=2.948717948717949 s^-1 mM^-1 from same-row quotient

row_label: L-Allose

substrate: L-allose


column_label: Table 2 row D-Mannose lists Km 946 +/- 7 mM, kcat 3748 +/- 240 s^-1, and kcat/Km 3.5 +/- 0.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=946 mM; kcat normalized=3748 s^-1; kcat/Km normalized=3.9619450317124736 s^-1 mM^-1 from same-row quotient

row_label: D-Mannose


organism: Geobacillus thermodenitrificans

substrate_name: D-galactose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C450S/N475K to reconstruct the assayed variant sequence.

substrate: D-galactose


sequence_variant_note: Mutation signature F280N/C450S/N475K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Aeropyrum pernix

substrate_name: D-fructose 6-phosphate

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

column_label: Table I row A. pernix PGI/PMI | F6P alternate 50 C value, Km block, reports 0.21 +/- 0.05 mM.

raw_value_unit_evidence: Table I A. pernix PGI/PMI | F6P alternate 50 C value, Km block, raw value 0.21 +/- 0.05 mM.

table_label: Table I. Molecular and kinetic properties of bifunctional PGI/PMI purified from A. pernix and recombinant PGI/PMI from T. acidophilum

substrate: D-fructose 6-phosphate


column_label: Table I row A. pernix PGI/PMI | M6P, Km block, reports 1.1 +/- 0.3 mM.

raw_value_unit_evidence: Table I A. pernix PGI/PMI | M6P, Km block, raw value 1.1 +/- 0.3 mM.

row_label: A. pernix PGI/PMI | M6P


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


substrate_name: D-Allose 6-phosphate

substrate: D-Allose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H99N to reconstruct the assayed variant sequence.


organism: Thermoplasma acidophilum

column_label: Table I row T. acidophilum PGI/PMI | F6P, Km block, reports 0.20 +/- 0.03 mM.

raw_value_unit_evidence: Table I T. acidophilum PGI/PMI | F6P, Km block, raw value 0.20 +/- 0.03 mM.

row_label: T. acidophilum PGI/PMI | F6P


column_label: Table I row T. acidophilum PGI/PMI | M6P, Km block, reports 0.25 +/- 0.03 mM.

raw_value_unit_evidence: Table I T. acidophilum PGI/PMI | M6P, Km block, raw value 0.25 +/- 0.03 mM.

row_label: T. acidophilum PGI/PMI | M6P


column_label: Table I; T. acidophilum column; Km block; F6P row; raw Km value 0.20 +/- 0.03 mM; normalized Km=0.2 mM.

raw_value_unit_evidence: Table I gives T. acidophilum F6P Km 0.20 +/- 0.03 mM.

row_label: T. acidophilum F6P row

table_label: PMID 14551194, Table I: Molecular and kinetic properties of bifunctional PGI/PMI


column_label: Table I; T. acidophilum column; Km block; M6P row; raw Km value 0.25 +/- 0.03 mM; normalized Km=0.25 mM.

raw_value_unit_evidence: Table I gives T. acidophilum M6P Km 0.25 +/- 0.03 mM.

row_label: T. acidophilum M6P row


organism: Bacillus halodurans

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E268K to reconstruct the assayed variant sequence.


column_label: Table I; A. pernix column; Km block; F6P row; raw Km value 0.21 +/- 0.05 mM; normalized Km=0.21 mM.

raw_value_unit_evidence: Table I gives A. pernix F6P Km 0.44 +/- 0.10 mM at 80 C and a separate 0.21 +/- 0.05 mM value explicitly labeled 50 C.

row_label: A. pernix F6P row, alternate 50 C value


column_label: Table I; A. pernix column; Km block; M6P row; raw Km value 1.1 +/- 0.3 mM; normalized Km=1.1 mM.

raw_value_unit_evidence: Table I gives A. pernix M6P Km 1.1 +/- 0.3 mM.

row_label: A. pernix M6P row


organism: Anoxybacillus flavithermus


organism: Streptomyces rubiginosus

substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


substrate_name: D-Xylose

substrate: D-Xylose


organism: Saccharomyces cerevisiae

substrate_name: D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R189K to reconstruct the assayed variant sequence.

substrate: D-Ribose 5-phosphate


organism: Vibrio sp.

substrate_name: D-glucose

substrate: D-glucose


organism: Pyrobaculum aerophilum


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Geobacillus stearothermophilus

substrate_name: L-arabinose

assay_conditions_summary: pH 7.5; buffer pH 7

column_label: Official ScienceDirect HTML Table 4 reports l-arabinose for B. stearothermophilus US100: Vmax 41.8 U/mg, Km 28.57 mM, kcat/Km 71.4 min^-1 mM^-1, reference This study; the exact cell does not equal the exported 28.42 mM.

raw_value_unit_evidence: Km raw_value=28.57 raw_unit=mM

row_label: l-arabinose / B. stearothermophilus US100

table_label: Table 4 - Kinetic properties of L-AIs from several organisms

substrate: L-arabinose


column_label: Official ScienceDirect HTML Table 4 reports d-galactose for B. stearothermophilus US100: Vmax 8.9 U/mg, Km 57 mM, kcat/Km 8.48 min^-1 mM^-1, reference This study.

raw_value_unit_evidence: Km raw_value=57 raw_unit=mM

row_label: d-galactose / B. stearothermophilus US100


organism: Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)

substrate_name: fructose 6-phosphate (at 50 degrees Celsius)


substrate_name: mannose 6-phosphate (at 80 degrees Celsius)


organism: Methanocaldococcus jannaschii


organism: Arabidopsis thaliana

column_label: The abstract reports the apparent Km for Man-6P of purified recombinant PMI2 was 372+/-13 microM.

raw_value_unit_evidence: Km raw_value=372+/-13 microM raw_unit=microM

row_label: Prose segment: PMI2 Man-6P Km

table_label: PubMed PMID 18755683 abstract


column_label: The abstract reports the apparent Km for Man-6P of purified recombinant PMI1 was 41.3+/-4.2 microM.

raw_value_unit_evidence: Km raw_value=41.3+/-4.2 microM raw_unit=microM

row_label: Prose segment: PMI1 Man-6P Km


substrate_name: glucose 6-phosphate (at 50 degrees Celsius)


substrate: fructose 6-phosphate (at 50 degrees Celsius)


organism: Mycobacterium tuberculosis


organism: Thermoanaerobacter mathranii

substrate_name: D-fucose

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

substrate: D-fucose


organism: Lactobacillus plantarum

substrate_name: D-Galactose

substrate: D-Galactose


substrate_name: L-Arabinose


organism: Lactobacillus sakei


organism: Rattus norvegicus

column_label: Abstract states apparent Km and Vmax were 0.593 +/- 0.031 mM and 2291 +/- 61 nmol/min/mg protein for glucose 6-phosphate.

raw_value_unit_evidence: Km raw_value=0.593 mM raw_unit=mM

row_label: Rat brain phosphoglucose isomerase / glucose 6-phosphate

table_label: PubMed XML abstract


column_label: Abstract states apparent Km and Vmax were 0.095 +/- 0.013 mM and 2035 +/- 98 nmol/min/mg protein for fructose 6-phosphate.

raw_value_unit_evidence: Km raw_value=0.095 mM raw_unit=mM

row_label: Rat brain phosphoglucose isomerase / fructose 6-phosphate


organism: Thermoanaerobacter ethanolicus

substrate_name: D-xylose

assay_conditions_summary: pH 7; buffer 100 mM MOPS

substrate: D-xylose


organism: Escherichia coli (strain K12)

substrate_name: D-allose 6-phosphate

substrate: D-allose 6-phosphate


organism: Pyrococcus furiosus

substrate_name: L-talose

proof_lines:
pH 7.0, 95°C
Raw SKiD Env: Temp=95°C, pH=7

substrate: L-talose


organism: [Clostridium] hylemonae

substrate_name: D-galactose


substrate_name: D-ribose 5-phosphate (at 37 degrees Celsius)


organism: Homo sapiens


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: fructose 6-phosphate

column_label: Table I; A. pernix column; Km block; F6P row; raw Km value 0.44 +/- 0.10 mM; normalized Km=0.44 mM.

raw_value_unit_evidence: Table I gives A. pernix F6P Km 0.44 +/- 0.10 mM.

row_label: A. pernix F6P row

substrate: fructose 6-phosphate


organism: Pseudoalteromonas haloplanktis

column_label: PubMed XML abstract PMID 27586234, same L-arabinose measurement: Km 111.68 mM; kcat 773.30 min^-1; kcat/Km 6.92 mM^-1 min^-1.

normalized_value_unit_evidence: Preserve catalog-rounded Km 111.7 mM and kcat 12.9 s^-1; normalize the independently printed ratio to 0.11533333333333333 s^-1 mM^-1.

raw_value_unit_evidence: PubMed abstract: Km 111.68 mM; kcat 773.30 min^-1; independently printed kcat/Km 6.92 mM^-1 min^-1.

row_label: recombinant Pseudoalteromonas haloplanktis L-arabinose isomerase / L-arabinose

table_label: PubMed XML abstract (no table)

substrate: L-Arabinose


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)


organism: Pseudomonas aeruginosa

substrate_name: D-Mannose 6-phosphate

substrate: D-Mannose 6-phosphate


organism: Saccharomyces cerevisiae


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


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


organism: Chlorella variabilis


organism: Oryctolagus cuniculus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycobacterium tuberculosis

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 7.6; buffer assay

column_label: PMID 17126561 Determination of kinetic constants/Fig. 5A, rPGI-His6 with fructose-6-phosphate, Km = 0.27 +/- 0.03 mM.

raw_value_unit_evidence: Kinetic constants prose/Fig. 5A reports Km = 0.27 +/- 0.03 mM for fructose-6-phosphate.

row_label: rPGI-His6 / fructose-6-phosphate

table_label: Determination of kinetic constants prose and Fig. 5A

substrate: D-fructose 6-phosphate


organism: Geobacillus thermodenitrificans

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


substrate: D-galactose


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


substrate_name: D-Glucose 6-phosphate

substrate: D-Glucose 6-phosphate


organism: Archaeoglobus fulgidus


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


organism: Alicyclobacillus hesperidum


substrate_name: L-arabinose


organism: Thermus thermophilus

substrate_name: D-glucose


substrate_name: D-glucose; D-mannose

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

substrate: D-glucose; D-mannose


substrate: D-glucose


substrate_name: Unknown

substrate: Unknown


organism: Limosilactobacillus fermentum

proof_lines: mutant enzyme D268K/D269K/D299K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D268K/D269K/D299K, at pH 4.0 and 65°C

proof_lines: mutant enzyme D268K/D269K/D299K, at pH 6.0 and 65°C


proof_lines: mutant enzyme D269K/D299K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D269K/D299K, at pH 6.0 and 65°C

proof_lines: mutant enzyme D269K/D299K, at pH 4.0 and 65°C


proof_lines:
wild type enzyme, at pH 6.0 and 65°C
wild type enzyme, at pH 5.0 and 65°C


proof_lines:
mutant enzyme D299K, at pH 5.0 and 65°C
mutant enzyme D299K, at pH 6.0 and 65°C
mutant enzyme D299K, at pH 4.0 and 65°C


proof_lines:
mutant enzyme D299R, at pH 5.0 and 65°C
mutant enzyme D299R, at pH 6.0 and 65°C
mutant enzyme D299R, at pH 4.0 and 65°C


proof_lines:
mutant enzyme D268K, at pH 6.0 and 65°C
mutant enzyme D268K, at pH 5.0 and 65°C
mutant enzyme D268K, at pH 4.0 and 65°C


proof_lines:
mutant enzyme D269K, at pH 6.0 and 65°C
mutant enzyme D269K, at pH 5.0 and 65°C
mutant enzyme D269K, at pH 4.0 and 65°C


proof_lines: mutant enzyme D268K/D269K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D268K/D269K, at pH 6.0 and 65°C

proof_lines: mutant enzyme D268K/D269K, at pH 4.0 and 65°C


proof_lines: mutant enzyme D268K/D299K, at pH 6.0 and 65°C

proof_lines: mutant enzyme D268K/D299K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D268K/D299K, at pH 4.0 and 65°C


substrate_name: D-glucose 6-phosphate

proof_lines: mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)

substrate: D-glucose 6-phosphate


proof_lines: mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)


organism: Actinoplanes missouriensis


proof_lines:
mutant H220Q
D-xylose, mutant H220Q


proof_lines:
mutant H220Q
D-glucose, mutant H220Q


proof_lines:
wild-type enzyme
wild-type


substrate_name: D-fructose

substrate: D-fructose


organism: Streptomyces pseudogriseolus

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, wild-type

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A and wild-type


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Thermococcus litoralis


proof_lines: 50°C, pH 7.5, D-fructose 6-phosphate as substrate


substrate_name: D-xylose

proof_lines: mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C