substrate_name: (S)-NADPHX

column_label: Supplemental Table S3, dehydratase substrate (S)-NADPHX, YjeF row, Km column cell 0.86 +/- 0.32 uM.

normalized_value_unit_evidence: 0.86 uM = 0.00086 mM; matches package/export Km 0.00086 mM.

raw_value_unit_evidence: Supplemental Table S3 reports Km units as uM; (S)-NADPHX row, YjeF enzyme: Km 0.86 +/- 0.32 uM.

row_label: YjeF / (S)-NADPHX

table_label: Supplemental Table S3

substrate: (S)-NADPHX


enzyme_display_name: NAD(P)H-hydrate epimerase

organism: Escherichia coli (strain K12)

substrate_name: ADP

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.1; cofactor ADP

column_label: Supplemental Table S3, ADP row, YjeF enzyme, Km column cell 3.6 +/- 1.1 uM.

raw_value_unit_evidence: Supplemental Table S3 reports Km units as uM; ADP row, YjeF enzyme: Km 3.6 +/- 1.1 uM.

row_label: YjeF / ADP

data_origin: experimental

enzyme: NAD(P)H-hydrate epimerase

substrate: ADP

status: verified

source: uniprot


organism: Escherichia coli

substrate_name: 7,8-dihydroneopterin 3'-triphosphate

source_db: brenda

verification_status: unverified

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

substrate: 7,8-dihydroneopterin 3'-triphosphate

status: unverified

source: brenda


organism: Salmonella typhi

substrate_name: UDP-GlcNAcA

verification_status: corrected

assay_conditions_summary: pH 8; buffer 40 uL of 50 mM potassium phosphate

column_label: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC Determined by the HPLC Assay and Capillary Electrophoresis Assay), substrate row 'UDP-GlcNAcA (4)b'; column 'Km (mM)' = 0.020; column 'Vmax (mM/min)' = 0.0015; column 'TviC mM' = 2.7 x 10^-5; column 'kcat (min-1)' = 56.8; column 'kcat/Km (mM-1min-1)' = 2871.6.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.020 mM; the printed column head is Km (mM), so no unit conversion applies and 0.02 mM is the canonical paper value. kcat: printed Table 2 cell 56.8 min^-1; the printed column head is kcat (min-1), and 1 min^-1 is 1/60 s^-1, so 56.8 / 60 = 0.9466666666666667 s^-1 is the canonical paper value. kcat/Km: printed Table 2 cell 2871.6 mM^-1 min^-1; the printed column head is kcat/Km (mM-1min-1), and 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 2871.6 / 60 = 47.86 s^-1 mM^-1 is the canonical paper value.

raw_value_unit_evidence: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC), substrate row 'UDP-GlcNAcA (4)b': Km = 0.020 mM; Vmax = 0.0015 mM/min; TviC = 2.7 x 10^-5 mM; kcat = 56.8 min^-1; printed kcat/Km = 2871.6 mM^-1 min^-1.

row_label: Table 2, substrate row 'UDP-GlcNAcA (4)b'

table_label: Table 2: Kinetic Parameters for Reactions Catalyzed by TviC Determined by the HPLC Assay and Capillary Electrophoresis Assay (Biochemistry 2006, 45(26): 8163-8173)

substrate: UDP-GlcNAcA

status: corrected


substrate_name: UDP-GalNAcA

column_label: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC Determined by the HPLC Assay and Capillary Electrophoresis Assay), substrate row 'UDP-GalNAcA (5)b'; column 'Km (mM)' = 0.042; column 'Vmax (mM/min)' = 0.0021; column 'TviC mM' = 5.3 x 10^-5; column 'kcat (min-1)' = 39.1; column 'kcat/Km (mM-1min-1)' = 931.3.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.042 mM; the printed column head is Km (mM), so no unit conversion applies and 0.042 mM is the canonical paper value. kcat: printed Table 2 cell 39.1 min^-1; the printed column head is kcat (min-1), and 1 min^-1 is 1/60 s^-1, so 39.1 / 60 = 0.6516666666666667 s^-1 is the canonical paper value. kcat/Km: printed Table 2 cell 931.3 mM^-1 min^-1; the printed column head is kcat/Km (mM-1min-1), and 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 931.3 / 60 = 15.521666666666667 s^-1 mM^-1 is the canonical paper value.

raw_value_unit_evidence: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC), substrate row 'UDP-GalNAcA (5)b': Km = 0.042 mM; Vmax = 0.0021 mM/min; TviC = 5.3 x 10^-5 mM; kcat = 39.1 min^-1; printed kcat/Km = 931.3 mM^-1 min^-1.

row_label: Table 2, substrate row 'UDP-GalNAcA (5)b'

substrate: UDP-GalNAcA


substrate_name: UDP-GlcNAc

proof_lines: kcat is 56.8 min(-1) with UDP-GlcNAcA as substrate. kcat is 39.1 min(-1) with UDP-GalNAcA as substrate. kcat is 14.2 min(-1) with UDP-GlcNAc as substrate. kcat is 52.6 min(-1) with UDP-GalNAc as substrate.

substrate: UDP-GlcNAc


enzyme_display_name: alpha-methylacyl-CoA racemase

organism: Rattus norvegicus

substrate_name: trihydroxycoprostanoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: alpha-methylacyl-CoA racemase

substrate: trihydroxycoprostanoyl-CoA


substrate_name: pristanoyl-CoA

substrate: pristanoyl-CoA


enzyme_display_name: maleate isomerase

organism: Pseudomonas sp.

substrate_name: Maleate

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

enzyme: maleate isomerase

substrate: Maleate


organism: Solanum lycopersicum

substrate_name: S-adenosyl-L-ethionine

substrate: S-adenosyl-L-ethionine


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Sphingobium chungbukense

substrate_name: alpha-D-mannose 1-phosphate

proof_lines: SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C

substrate: alpha-D-mannose 1-phosphate


enzyme_display_name: phosphomannomutase

substrate_name: alpha-D-glucose 1-phosphate

enzyme: phosphomannomutase

substrate: alpha-D-glucose 1-phosphate


organism: Homo sapiens

substrate_name: (S)-naproxenoyl-CoA

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH and temperature not specified in the publication

proof_lines: anti-enantiomer, pH not specified in the publication, temperature not specified in the publication

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

substrate: (S)-naproxenoyl-CoA


assay_conditions_summary: pH 7.2; cofactor CoA

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

proof_lines: recombinant enzyme, 50 mM NaH2PO4-NaOH, pH 7.2


enzyme_display_name: alanine racemase

organism: Staphylococcus aureus

substrate_name: D-alanine

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

proof_lines: pH not specified in the publication, 30°C, recombinant enzyme

enzyme: alanine racemase

substrate: D-alanine


enzyme_display_name: L-3-cyanoalanine synthase

organism: Spinacia oleracea

substrate_name: KCN

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

enzyme: L-3-cyanoalanine synthase

substrate: KCN


organism: Streptomyces lavendulae

substrate_name: D-serine

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

substrate: D-serine


substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: hydantoin racemase

enzyme: hydantoin racemase


enzyme_display_name: maleylpyruvate isomerase

organism: Corynebacterium glutamicum

enzyme: maleylpyruvate isomerase


enzyme_display_name: linoleate isomerase

organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: 9-cis,12-cis-linoleic acid

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

enzyme: linoleate isomerase

substrate: 9-cis,12-cis-linoleic acid


organism: Butyrivibrio fibrisolvens

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


organism: Mus musculus

substrate_name: (R)-NADPHX

substrate: (R)-NADPHX


organism: Rhizobium meliloti

substrate_name: D-5-isobutylhydantoin (D-IBH)

proof_lines: kcat is 6.42 sec(-1) with L-5-ethylhydantoin (L-EH) as substrate. kcat is 3.24 sec(-1) with D-5-isobutylhydantoin (D-IBH) as substrate. kcat is 2.29 sec(-1) with D-5-benzylhydantoin (D-BH) as substrate. kcat is 2.12 sec(-1) with L-5-isobuty

substrate: D-5-isobutylhydantoin (D-IBH)


substrate_name: L-5-benzylhydantoin (L-BH)

substrate: L-5-benzylhydantoin (L-BH)


enzyme_display_name: maleylacetoacetate isomerase

organism: Arabidopsis thaliana

enzyme: maleylacetoacetate isomerase


enzyme_display_name: 7,8-dihydroneopterin epimerase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 7,8-dihydroneopterin in the aldolase reaction

proof_lines: kcat is 0.0054 sec(-1) for the aldolase reaction with 7,8-dihydroneopterin as substrate. kcat is 0.006 sec(-1) for the aldolase reaction with 7,8-dihydromonapterin as substrate. kcat is 0.0015 sec(-1) for the epimerization of 7,8-dihydroneo

enzyme: 7,8-dihydroneopterin epimerase


organism: Alicyclobacillus acidoterrestris


substrate_name: dichloroacetic acid

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

substrate: dichloroacetic acid


substrate_name: glutathione

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

column_label: Abstract states the Km for glutathione was 59 microM.

raw_value_unit_evidence: Km raw_value=59 raw_unit=microM

row_label: rat liver glutathione transferase zeta with glutathione

table_label: PubMed abstract PMID 9531472

substrate: glutathione


organism: Clostridium sporogenes


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


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


organism: Pseudomonas aeruginosa

substrate_name: UDP-N-acetylgalactosamine

proof_lines: kcat is 271 min(-1) with UDP-N-acetylgalactosamine as substrate. kcat is 120 min(-1) with UDP-N-acetylglucosamine as substrate. kcat is 0.188 min(-1) with UDP-galactose as substrate. kcat is 0.124 min(-1) with UDP-glucose as substrate.

substrate: UDP-N-acetylgalactosamine


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Escherichia coli (strain K12)

substrate_name: 7,8-dihydroneopterin in aldolase reaction


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate: 7,8-dihydroneopterin in aldolase reaction


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

mutation_type: substitution


proof_lines:
pH 7.6, 25°C, enzyme hGSTZ1d-1d
pH 7.6, 25°C, enzyme hGSTZ1c-1c
pH 7.6, 25°C, enzyme hGSTZ1b-1b


organism: Nocardia farcinica

substrate_name: Maleate

proof_lines: mutant enzyme C194S, at pH 7.5, temperature not specified in the publication

substrate: Maleate


proof_lines: mutant enzyme C76S, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme Y133F, at pH 7.5, temperature not specified in the publication


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


substrate_name: Unknown

proof_lines: pH 7.5, temperature not specified in the publication

substrate: Unknown


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


substrate_name: O-acetyl-L-serine

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

proof_lines:
26°C, pH 9.8
vs. chloroalanine

substrate: O-acetyl-L-serine


organism: Escherichia coli

substrate_name: 7,8-dihydroneopterin triphosphate

substrate: 7,8-dihydroneopterin triphosphate


organism: Synechococcus sp.


organism: Homo sapiens

substrate_name: trihydroxycoprostanoyl-CoA

substrate: trihydroxycoprostanoyl-CoA


substrate_name: pristanoyl-CoA

substrate: pristanoyl-CoA


enzyme_display_name: chorismate mutase

organism: Thermus thermophilus

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: methionine gamma-lyase

organism: Trichomonas vaginalis

substrate_name: DL-homocysteine

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

enzyme: methionine gamma-lyase

substrate: DL-homocysteine


substrate_name: L-cysteine

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

substrate: L-cysteine


organism: Serratia marcescens


substrate_name: L-ethionine

substrate: L-ethionine


substrate_name: L-methionine

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

substrate: L-methionine


enzyme_display_name: phosphoacetylglucosamine mutase

organism: Trypanosoma brucei

substrate_name: N-acetyl-D-glucosamine 6-phosphate

enzyme: phosphoacetylglucosamine mutase

substrate: N-acetyl-D-glucosamine 6-phosphate


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


organism: Alcaligenes faecalis

source_db: oed

source: oed


substrate_name: maleate

substrate: maleate


organism: Trypanosoma cruzi


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


enzyme_display_name: protoporphyrin ferrochelatase

organism: Xenopus laevis

substrate_name: protoporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin


organism: Ralstonia sp.

substrate_name: maleylpyruvate

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R109A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 50 mM phosphate

proof_lines: mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22°C

substrate: maleylpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R8A/R176A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H104A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q49A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R8A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N108A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22°C


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

proof_lines: mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C


proof_lines: wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T11A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22°C


enzyme_display_name: S-ribosylhomocysteine lyase

organism: Vibrio cholerae

proof_lines: pH and temperature not specified in the publication

enzyme: S-ribosylhomocysteine lyase


enzyme_display_name: lactoylglutathione lyase

organism: Sus scrofa

substrate_name: Phenylglyoxal

enzyme: lactoylglutathione lyase

substrate: Phenylglyoxal


substrate_name: methylglyoxal

substrate: methylglyoxal


organism: Yersinia pestis

smiles: CC(=O)C=O

assay_conditions_summary: pH 7

proof_lines:
presence of Co2+, pH 7.0
presence of Ni2+, pH 7.0


substrate_name: (R)-S-lactoylglutathione

proof_lines:
pH 7.0, 0.5 mM CoCl2
pH 7.0, 0.5 mM NiCl2

substrate: (R)-S-lactoylglutathione


substrate_name: Maleate

source_db: skid

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

sequence_source: multiple

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
kcat is 2.8 sec(-1).

source_databases_merged: skid uniprot

substrate: Maleate

source: skid


enzyme_display_name: proline racemase

substrate_name: L-proline

enzyme: proline racemase

substrate: L-proline


substrate_name: Unknown

proof_lines: recombinant His-tagged enzyme, pH 6.0, 37°C

substrate: Unknown


enzyme_display_name: alpha-methylacyl-CoA racemase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 3.7 sec(-1) with (25R)-3-oxo-cholest-4-en-26-oyl-CoA as substrate (PubMed:26348625). kcat is 450 sec(-1) with (2S)-ibuprofenoyl-CoA as substrate (PubMed:19854148). kcat is 291 sec(-1) with (2R)-ibuprofenoyl-CoA as substrate (PubMed:

enzyme: alpha-methylacyl-CoA racemase


enzyme_display_name: D-ornithine 4,5-aminomutase

organism: Acetoanaerobium sticklandii

substrate_name: D-ornithine

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

enzyme: D-ornithine 4,5-aminomutase

substrate: D-ornithine


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


enzyme_display_name: lysine 5,6-aminomutase

substrate_name: D-Lysine

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

proof_lines: with pyridoxal 5'-phosphate N-oxide as cofactor, pH 8.5, 37°C

proof_lines: with pyridoxal 5'-phosphate as cofactor, pH 8.5, 37°C

enzyme: lysine 5,6-aminomutase

substrate: D-Lysine


enzyme_display_name: triose-phosphate isomerase

organism: Oryctolagus cuniculus

substrate_name: D-glyceraldehyde 3-phosphate

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

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: UniProt P00940

organism: Gallus gallus

substrate_name: dihydroxyacetone 3-phosphate

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P00940

substrate: dihydroxyacetone 3-phosphate


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.6
Raw SKiD Env: Temp=25°C, pH=7.5


enzyme_display_name: UniProt P36186

organism: Giardia intestinalis

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.4

enzyme: UniProt P36186


enzyme_display_name: UniProt P04789

enzyme: UniProt P04789


enzyme_display_name: UniProt A2FT29

enzyme: UniProt A2FT29


enzyme_display_name: UDP-glucuronate 4-epimerase

organism: Zea mays

substrate_name: UDP-glucuronate

proof_lines: recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, in 0.1 M sodium phosphate, pH 7.6

enzyme: UDP-glucuronate 4-epimerase

substrate: UDP-glucuronate


proof_lines: recombinant ZmUGlcAE, position 1-47 is lacking


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


organism: Vibrio vulnificus

proof_lines: in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C


enzyme_display_name: alanine racemase

organism: Acinetobacter baumannii

substrate_name: D-alanine

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

proof_lines: pH not specified in the publication, 30°C

enzyme: alanine racemase

substrate: D-alanine


enzyme_display_name: chorismate mutase

organism: Acinetobacter calcoaceticus

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


organism: Lathyrus oleraceus


substrate_name: glycerone phosphate

substrate: glycerone phosphate


organism: Pteris vittata


organism: Homo sapiens

proof_lines:
isoenzyme B
isoenzyme A
enzyme form III


substrate_name: L-Pro

substrate: L-Pro


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208T/S211G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S211G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K17L/Y46F/D48F/Q82F/D85L to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K17L/Y46F/D48Y/Q82A/D85A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K17P/Y46A/D48L/Q82T/D85A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K17A/Y46A/D48F/Q82A/D85S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: dihydroxyacetone phosphate

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

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


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

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


organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)

substrate_name: D-glyceraldehyde-3-phosphate (at pH 7.4)

proof_lines: kcat is 4016 sec(-1) with D-glyceraldehyde-3-phosphate as substrate (at pH 7.4).


organism: Chlamydomonas reinhardtii

proof_lines: in 100 mM triethanolamine (pH 7.4), at 25°C


organism: Moritella marina

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A238S to reconstruct the assayed variant sequence.

proof_lines:
pH 7.6, mutant enzyme A238S
mutant A238S


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

proof_lines: kcat is 420000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at pH 7.6 and 10 degrees Celsius).


organism: Giardia duodenalis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W162F with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


organism: Helicobacter pylori

proof_lines: kcat is 88000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at pH 7.5 and 25 degrees Celsius).


organism: Escherichia coli (strain K12)

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

proof_lines: kcat is 54000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at 25 degrees Celsius).


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

proof_lines:
active form P2 of TIM, at 25°C, pH 7.4
isoenzyme A
active form P1 of TIM, at 25°C, pH 7.4


organism: Trichomonas vaginalis

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K12G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C


organism: Trypanosoma

substrate_name: D-Glyceraldehyde 3-phosphate

substrate: D-Glyceraldehyde 3-phosphate


organism: Escherichia coli


organism: Mycobacterium tuberculosis

proof_lines: kcat is 4.3 min(-1) for isomerase activity.


organism: Gallus gallus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V167G/W168G/K174G/T175G/A176G to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K174G/T175G/A176G to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 7.6, mutant enzyme K174G/T175G/A176G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V167G/W168G to reconstruct the assayed variant sequence.


enzyme_display_name: peptidylprolyl isomerase

substrate_name: RNase T1

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V72P to reconstruct the assayed variant sequence.

proof_lines: mutant V72P, pH not specified in the publication, temperature not specified in the publication

enzyme: peptidylprolyl isomerase

substrate: RNase T1


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I65P to reconstruct the assayed variant sequence.

proof_lines: mutant I65P, pH not specified in the publication, temperature not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K63A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C113D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R68A/R69A to reconstruct the assayed variant sequence.


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

proof_lines: kcat is 5668 sec(-1) for isomerase activity.


organism: Tenebrio molitor


organism: Thermococcus onnurineus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Oryctolagus cuniculus


organism: Pyrococcus furiosus

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -15, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 8


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


organism: Saccharolobus solfataricus


organism: Mycoplasmoides genitalium


sequence_variant_note: Mutation signature S54G/P55N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: disulfide-reduced and S-carboxymethylated form of a variant of Rnase T1 with Ser54Gly and Pro55Asn


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D205G with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

proof_lines: 20°C, pH 7.4, mutant D205G of Ypa1, presence of 1 mM MgATP


organism: Clostridium perfringens (strain 13 / Type A)

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

proof_lines: kcat is 6348 sec(-1) for isomerase activity.


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

proof_lines: kcat is 5678 sec(-1) for isomerase activity.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208T/S211G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y208T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K12G to reconstruct the assayed variant sequence.


proof_lines: wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C


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

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S211G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V167G/W168G/K174G/T175G/A176G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V167G/W168G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K174G/T175G/A176G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I45Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I45F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I45G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I45A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I45V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I45L 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: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines:
25°C, pH 7.4, wild-type enzyme
wild-type, pH 7.5, 25°C


sequence_variant_note: Mutation signature C126A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature 173del to reconstruct the assayed variant sequence.

mutation_type: deletion


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


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature C127S to reconstruct the assayed variant sequence.

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature C127S/C218S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature C218S to reconstruct the assayed variant sequence.


row_label: WT


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D/E97D with inferred residue-numbering offset -20 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D/G10S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D/G233R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D/S96P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D/S96T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165D/V167D with inferred residue-numbering offset -25 to reconstruct the assayed variant sequence.


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


proof_lines: The kcat is 900 sec(-1) for the isomerization of dihydroxyacetone phosphate (PubMed:2021650). The kcat is 0.011 sec(-1) for the production of methylglyoxal via the elimination reaction (PubMed:2021650). Produces methylglyoxal with a calcula

source_databases_merged: brenda uniprot


organism: Plasmodium falciparum

proof_lines: kcat is 4300 sec(-1) with D-glyceraldehyde-3-phosphate as substrate (at 25 degrees Celsius) (PubMed:26762569). kcat is 4233 sec(-1) with D-glyceraldehyde-3-phosphate as substrate (at pH 7.6) (PubMed:19622869).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C126A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C126M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C126S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C126T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C126V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S211G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y208A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y208F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y208S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y208T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y208T/S211G to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D225Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T75S with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T75V with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T75C with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T75N with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


organism: Trypanosoma cruzi

sequence_variant_note: Mutation signature S20Q/L47V/I49L/P50A/Y87F/I89V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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 E165A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E97Q to reconstruct the assayed variant sequence.


organism: Clostridium perfringens


column_label: Table 2 reports KM 8.4 x 10^-4 M, kcat 4300 s^-1, and catalytic efficiency 5.1 x 10^6 s^-1 M^-1 for Tenebrio molitor TIM.

normalized_value_unit_evidence: Km normalized_value=0.84 normalized_unit=mM; kcat normalized_value=4300 normalized_unit=s^-1; kcat/Km normalized_value=5100 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=8.4 x 10^-4 raw_unit=M; kcat raw_value=4300 raw_unit=s^-1; kcat/Km raw_value=5.1 x 10^6 raw_unit=s^-1 M^-1

row_label: Tenebrio molitor / glyceraldehyde 3-phosphate

table_label: Wiley Table 2, kinetic parameters for Tenebrio molitor TIM


enzyme_display_name: beta-carotene isomerase

organism: Oryza sativa Japonica Group

column_label: Chrome-visible Wiley full text states: The KM for 9-cis-beta-carotene in the reverse reaction was determined to be 0.26 uM, with a kcat value of 34 s^-1.

raw_value_unit_evidence: KM raw_value=0.26 uM raw_unit=uM

row_label: OsD27 reverse reaction / 9-cis-beta-carotene

table_label: Wiley/FEBS Journal full text prose / Biochemical characterization of OsD27

enzyme: beta-carotene isomerase


organism: Homo sapiens

substrate_name: Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide

substrate: Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide


column_label: Results text reports kcat 960 s^-1 and Km 230 microM for the tetrapeptide substrate; 230 microM converts to 0.23 mM.

raw_value_unit_evidence: Km raw_value=230 microM raw_unit=microM

row_label: Human PPIL1 recombinant enzyme / N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide

table_label: JBC full text PMID 16595688 Results / PPIase activity assay


organism: Nostoc punctiforme


organism: Rattus norvegicus


organism: Deinococcus radiodurans


organism: Trichomonas vaginalis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I45A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature I45F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


sequence_variant_note: Mutation signature I45L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I45V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I45Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


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

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


organism: Gemmata obscuriglobus

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


organism: Gallus gallus


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

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


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


organism: Trypanosoma brucei brucei


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


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.


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


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


organism: Plasmodium falciparum

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


organism: Thermus thermophilus

substrate_name: TRYWNAKMK-(cis)-PFIFGA

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

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


organism: Aeromonas hydrophila subsp. hydrophila

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


organism: Trypanosoma brucei brucei

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


substrate_name: D-glyceraldehyde 3-phosphate


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


organism: Amborella trichopoda

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


organism: Alkalihalophilus pseudofirmus

substrate_name: D-alanine / L-alanine

substrate: D-alanine / L-alanine


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Arabidopsis thaliana

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

substrate_name: chorismate

enzyme: isochorismate synthase


substrate_name: D-alanine

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


substrate: Unknown


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.

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


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

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


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13375 and applied mutation signature H311Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic constants of wild-type and mutant phosphoglucose isomerase), enzyme row 'H311Q'; column 'KM Fructose-6-P (mM)' = 18; column 'kcat (s^-1)' = 5.0; column 'kcat/KM (s^-1 mM^-1)' = 0.28.

normalized_value_unit_evidence: Km: printed Table 1 cell 18 mM; already in mM, so no unit conversion applies; the catalog value is 18.0 mM. kcat: printed Table 1 cell 5.0 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 5.0 s^(-1). kcat/Km: printed Table 1 cell 0.28 s^-1 mM^-1; already in s^-1 mM^-1, so no unit conversion applies. The quotient of the two printed component cells is 5.0 / 18 = 0.2777777777777778 s^-1 mM^-1, which is the catalog value; the printed cell 0.28 is that same quotient carried to the two significant figures the table prints, and the exact quotient lies inside the rounding interval of the printed cell.

raw_value_unit_evidence: Table 1, enzyme row 'H311Q': column 'KM Fructose-6-P (mM)' = 18; column 'kcat (s^-1)' = 5.0; column 'kcat/KM (s^-1 mM^-1)' = 0.28.

row_label: Table 1, enzyme row 'H311Q'

table_label: Table 1. Kinetic constants of wild-type and mutant phosphoglucose isomerase (Protein Science 1999, 8:2438-2443)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13375 and applied mutation signature H311N to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic constants of wild-type and mutant phosphoglucose isomerase), enzyme row 'H311N'; column 'KM Fructose-6-P (mM)' = 2.1; column 'kcat (s^-1)' = 1.1; column 'kcat/KM (s^-1 mM^-1)' = 0.52.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.1 mM; already in mM, so no unit conversion applies; the catalog value is 2.1 mM. kcat: printed Table 1 cell 1.1 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 1.1 s^(-1). kcat/Km: printed Table 1 cell 0.52 s^-1 mM^-1; already in s^-1 mM^-1, so no unit conversion applies. The quotient of the two printed component cells is 1.1 / 2.1 = 0.5238095238095238 s^-1 mM^-1, which is the catalog value; the printed cell 0.52 is that same quotient carried to the two significant figures the table prints, and the exact quotient lies inside the rounding interval of the printed cell.

raw_value_unit_evidence: Table 1, enzyme row 'H311N': column 'KM Fructose-6-P (mM)' = 2.1; column 'kcat (s^-1)' = 1.1; column 'kcat/KM (s^-1 mM^-1)' = 0.52.

row_label: Table 1, enzyme row 'H311N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13375 and applied mutation signature H311A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic constants of wild-type and mutant phosphoglucose isomerase), enzyme row 'H311A'; column 'KM Fructose-6-P (mM)' = 0.38; column 'kcat (s^-1)' = 0.09; column 'kcat/KM (s^-1 mM^-1)' = 0.24.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.38 mM; already in mM, so no unit conversion applies; the catalog value is 0.38 mM. kcat: printed Table 1 cell 0.09 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 0.09 s^(-1). kcat/Km: printed Table 1 cell 0.24 s^-1 mM^-1; already in s^-1 mM^-1, so no unit conversion applies. The quotient of the two printed component cells is 0.09 / 0.38 = 0.23684210526315788 s^-1 mM^-1, which is the catalog value; the printed cell 0.24 is that same quotient carried to the two significant figures the table prints, and the exact quotient lies inside the rounding interval of the printed cell.

raw_value_unit_evidence: Table 1, enzyme row 'H311A': column 'KM Fructose-6-P (mM)' = 0.38; column 'kcat (s^-1)' = 0.09; column 'kcat/KM (s^-1 mM^-1)' = 0.24.

row_label: Table 1, enzyme row 'H311A'


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

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


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.


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)


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: 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.

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

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

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).


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.


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.