substrate_name: L-Ala-D-Glu

column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Glu. Enzyme column group: YcjG (E. coli). Columns read: KM (M) cell (1.3 ± 0.3) × 10-4, kcat (s-1) cell 10 ± 0.4, kcat/KM (M-1 s-1) cell 7.7 × 104. KM (1.3 ± 0.3) × 10-4 M normalizes to 0.13 mM and equals the exported km; kcat 10 ± 0.4 s^-1 normalizes to 10 s^-1 and equals the exported kcat; the exported kcat_over_km 76.92307692307692 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 7.7 × 104 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YcjG (E. coli) columns of row l-Ala-d-Glu: KM (1.3 ± 0.3) × 10-4 M = 0.13 mM; kcat 10 ± 0.4 s^-1 = 10 s^-1; kcat/KM taken as the quotient of those two printed cells, 10 s^-1 / 0.13 mM = 76.92307692307692 s^-1 mM^-1, which the table prints rounded to two significant figures as 7.7 × 104 M-1 s-1.

raw_value_unit_evidence: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB | column header: substrate	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M)	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M) | row: l-Ala-d-Glu	(1.3 ± 0.3) × 10-4	10 ± 0.4	7.7 × 104	−	(3.2 ± 1.1) × 10-4	15 ± 2.7	4.7 × 104	2.0 × 10-3

row_label: YcjG (E. coli) | l-Ala-d-Glu

substrate: L-Ala-D-Glu


enzyme_display_name: L-Ala-D/L-Glu epimerase

organism: Escherichia coli

substrate_name: L-Ala-D-Met

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADH

column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Met. Enzyme column group: YcjG (E. coli). Columns read: KM (M) cell (6.9 ± 0.4) × 10-4, kcat (s-1) cell 1.9 ± 0.1, kcat/KM (M-1 s-1) cell 2.8 × 103. KM (6.9 ± 0.4) × 10-4 M normalizes to 0.69 mM and equals the exported km; kcat 1.9 ± 0.1 s^-1 normalizes to 1.9 s^-1 and equals the exported kcat; the exported kcat_over_km 2.7536231884057973 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 2.8 × 103 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YcjG (E. coli) columns of row l-Ala-d-Met: KM (6.9 ± 0.4) × 10-4 M = 0.69 mM; kcat 1.9 ± 0.1 s^-1 = 1.9 s^-1; kcat/KM taken as the quotient of those two printed cells, 1.9 s^-1 / 0.69 mM = 2.7536231884057973 s^-1 mM^-1, which the table prints rounded to two significant figures as 2.8 × 103 M-1 s-1.

raw_value_unit_evidence: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB | column header: substrate	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M)	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M) | row: l-Ala-d-Met	(6.9 ± 0.4) × 10-4	1.9 ± 0.1	2.8 × 103	2.1 × 10-3	(5.1 ± 1.7) × 10-4	1.1 ± 0.1	2.2 × 103	−

row_label: YcjG (E. coli) | l-Ala-d-Met

data_origin: experimental

enzyme: L-Ala-D/L-Glu epimerase

substrate: L-Ala-D-Met

status: verified

source: oed


enzyme_display_name: 4-hydroxyproline epimerase

organism: Labrenzia aggregata

verification_status: corrected

assay_conditions_summary: pH 8; 298.15 K; buffer pH 8

column_label: Official eLife HTML Table 2 row SIAM614_28492 / A0NXQ7 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=55 normalized_unit=s^-1; Km normalized_value=3.2 normalized_unit=mM; kcat/KM normalized_value=17 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=55 +/- 3 raw_unit=s^-1; Km raw_value=3.2 +/- 0.5 raw_unit=mM; kcat/KM raw_value=17000 raw_unit=M^-1 s^-1

table_label: Table 2. Kinetic constants for 3/4HypE and t3HypD activities of the screened PRS targets

enzyme: 4-hydroxyproline epimerase

status: corrected


enzyme_display_name: serine racemase

organism: Homo sapiens

substrate_name: L-serine

source_db: skid

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

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

source_databases_merged: skid uniprot

enzyme: serine racemase

substrate: L-serine

source: skid


organism: Rattus norvegicus

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

source: uniprot


organism: Labrenzia alexandrii

column_label: Official eLife HTML Table 2 row SADFL11_2813 / B9R4E3 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=67 normalized_unit=s^-1; Km normalized_value=4.1 normalized_unit=mM; kcat/KM normalized_value=16 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=67 +/- 5 raw_unit=s^-1; Km raw_value=4.1 +/- 0.8 raw_unit=mM; kcat/KM raw_value=16000 raw_unit=M^-1 s^-1


organism: Caenorhabditis elegans


organism: Chromohalobacter salexigens

row_label: Csal_2339 / Q1QV19 / 4HypE

table_label: Table 2


organism: Paracoccus denitrificans

column_label: Official eLife HTML Table 2 row Pden_4859 / A1BBM5 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=16 normalized_unit=s^-1; Km normalized_value=25 normalized_unit=mM; kcat/KM normalized_value=0.63 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=16 +/- 2 raw_unit=s^-1; Km raw_value=25 +/- 5 raw_unit=mM; kcat/KM raw_value=630 raw_unit=M^-1 s^-1

row_label: Pden_4859 / A1BBM5 / 4HypE


organism: Rhizobium meliloti

column_label: Table 2 (PDF page 9 of 32); cluster 3; row group `SM_b20270 | Q92WR9`; Function sub-row `4HypE`; columns kcat [s-1] = `0.089`, KM [mM] = `6.3`, kcat/KM[M-1s-1] = `14`.

normalized_value_unit_evidence: kcat: printed cell 0.089 s^-1 -> 0.089 s^(-1); the export holds 0.089 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 6.3 mM -> 6.3 mM; the export holds 6.3 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 14 M^-1 s^-1 converted as 14 / 1000 = 0.014 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.014126984126984127 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `SM_b20270 | Q92WR9`, sub-row `4HypE`: kcat = 0.089 s^-1; KM = 6.3 mM; kcat/KM = 14 M^-1 s^-1.

row_label: SM_b20270 | Q92WR9 / 4HypE (Table 2 cluster 3)


source_db: brenda

verification_status: unverified

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

mutation_type: substitution

status: unverified

source: brenda


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

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


organism: Bacillus subtilis

substrate_name: L-Ala-D-Asp

substrate: L-Ala-D-Asp


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


substrate_name: L-Ala-D-Gln

substrate: L-Ala-D-Gln


organism: Shewanella loihica

column_label: Official eLife HTML Table 2 row Shew_2363 / A3QFI1 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=50 normalized_unit=s^-1; Km normalized_value=12 normalized_unit=mM; kcat/KM normalized_value=4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=50 +/- 6 raw_unit=s^-1; Km raw_value=12 +/- 3 raw_unit=mM; kcat/KM raw_value=4000 raw_unit=M^-1 s^-1

row_label: Shew_2363 / A3QFI1 / 4HypE


organism: Mus musculus

proof_lines: pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S


substrate_name: D-serine

proof_lines: pH 8.0, 30°C, recombinant mutant H150S/P151S

substrate: D-serine


proof_lines: pH 8.0, 30°C, recombinant mutant P151S/N152S


proof_lines: pH 8.0, 30°C, recombinant mutant H150S/N152S


enzyme_display_name: aspartate racemase

organism: Microcystis aeruginosa

substrate_name: L-aspartate

enzyme: aspartate racemase

substrate: L-aspartate


enzyme_display_name: L-dopachrome isomerase

substrate_name: dopachrome

enzyme: L-dopachrome isomerase

substrate: dopachrome


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Magallana gigas

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme


proof_lines: pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S


enzyme_display_name: protoporphyrin ferrochelatase

enzyme: protoporphyrin ferrochelatase


substrate_name: protoporphyrin

substrate: protoporphyrin


enzyme_display_name: phosphoenolpyruvate mutase

organism: Mytilus edulis

substrate_name: Phosphonopyruvate

enzyme: phosphoenolpyruvate mutase

substrate: Phosphonopyruvate


enzyme_display_name: alanine racemase

organism: Mycobacterium tuberculosis

substrate_name: L-alanine

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

enzyme: alanine racemase

substrate: L-alanine


enzyme_display_name: glutamate racemase

substrate_name: D-glutamate

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

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: UniProt P11444

organism: Pseudomonas putida

substrate_name: (S)-Mandelate

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P11444

substrate: (S)-Mandelate


substrate_name: (R)-mandelamide

substrate: (R)-mandelamide


enzyme_display_name: UDP-galactopyranose mutase

substrate_name: UDP-alpha-D-galactofuranose

enzyme: UDP-galactopyranose mutase

substrate: UDP-alpha-D-galactofuranose


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


substrate_name: L-serine O-sulfate

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

substrate: L-serine O-sulfate


enzyme_display_name: lactoylglutathione lyase

organism: Neisseria meningitidis

substrate_name: methylglyoxal

smiles: CC(=O)C=O

assay_conditions_summary: pH 7

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

enzyme: lactoylglutathione lyase

substrate: methylglyoxal


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


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

proof_lines:
mutant N122A, pH 7.5, 25°C
mutant enzyme N122A, at pH 7.5 and 25°C
mutant N122A, 25°C, pH 7.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K120A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines:
mutant K120A, pH 7.5, 25°C
mutant enzyme K120A, at pH 7.5 and 25°C


enzyme_display_name: phosphomannomutase

organism: Oryctolagus cuniculus

substrate_name: D-Glucose 1-phosphate

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

enzyme: phosphomannomutase

substrate: D-Glucose 1-phosphate


substrate_name: mannose 6-phosphate

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

substrate: mannose 6-phosphate


assay_conditions_summary: pH 8

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


enzyme_display_name: lactate racemase

organism: Latilactobacillus curvatus

substrate_name: D-lactate

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

enzyme: lactate racemase

substrate: D-lactate


substrate_name: L-lactate

substrate: L-lactate


substrate_name: D-serine

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: wild-type, racemization, presence of ATP, pH 7.4, 37°C

substrate: D-serine


proof_lines: mutant Q155D, racemization, pH 7.4, 37°C

proof_lines: mutant Q155D, racemization, presence of ATP, pH 7.4, 37°C

proof_lines: mutant Q155D, presence of ATP, pH 7.4, 37°C


enzyme_display_name: adenylate cyclase

substrate_name: ATP

assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines: cortical adenylyl cyclase, in the presence of 7 mM Mg2+, at 30°C, pH not specified in the publication

proof_lines: medulla adenylyl cyclase, in the presence of 7 mM Mg2+, at 30°C, pH not specified in the publication

enzyme: adenylate cyclase

substrate: ATP


substrate_name: Unknown

proof_lines: cortical adenylyl cyclase, in the presence of 7 mM Mn2+, at 30°C, pH not specified in the publication

proof_lines: medulla adenylyl cyclase, in the presence of 7 mM Mn2+, at 30°C, pH not specified in the publication

substrate: Unknown


organism: Latilactobacillus sakei


enzyme_display_name: histidine racemase

organism: Leuconostoc mesenteroides subsp. mesenteroides

substrate_name: L-histidine

enzyme: histidine racemase

substrate: L-histidine


enzyme_display_name: 4-hydroxyproline betaine 2-epimerase

organism: Salipiger bermudensis

substrate_name: L-proline betaine

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

proof_lines: kcat is 330 sec(-1) with trans-4-hydroxy-L-proline betaine as substrate and 5.3 sec(-1) with L-proline betaine as substrate.

source_databases_merged: brenda skid uniprot

enzyme: 4-hydroxyproline betaine 2-epimerase

substrate: L-proline betaine


substrate_name: trans-4-hydroxy-L-proline betaine

substrate: trans-4-hydroxy-L-proline betaine


organism: Paracoccus denitrificans (strain Pd 1222)

proof_lines: kcat is 110 sec(-1) with trans-4-hydroxy-L-proline betaine as substrate (PubMed:24056934). kcat is 68 sec(-1) with L-proline betaine as substrate (PubMed:24056934). kcat is 28 sec(-1) with D-proline betaine as substrate (PubMed:24520058).


enzyme_display_name: isoleucine 2-epimerase

organism: Arabidopsis thaliana

substrate_name: L-isoleucine

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

proof_lines: recombinant His-tagged enzyme, pH 8.0, 22°C

enzyme: isoleucine 2-epimerase

substrate: L-isoleucine


organism: Lentilactobacillus buchneri

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D222N with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D222N, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D222A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D222A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y142F to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant Y142F, pH and temperature not specified in the publication


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


sequence_source: multiple

proof_lines:
pH 5.5, 37°C
Raw SKiD Env: Temp=37°C, pH=5.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032)

proof_lines: kcat is 986 sec(-1) for conversion of L-lactate to D-lactate. kcat is 551 sec(-1) for conversion of D-lactate to L-lactate.


enzyme_display_name: mandelate racemase

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

enzyme: mandelate racemase


enzyme_display_name: 3-hydroxybutyryl-CoA epimerase

organism: Escherichia coli (strain K12)

substrate_name: L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)

assay_conditions_summary: cofactor CoA

enzyme: 3-hydroxybutyryl-CoA epimerase


organism: Fusobacterium nucleatum subsp. nucleatum (strain ATCC 23726 / VPI 4351)

proof_lines: kcat is 42 sec(-1) with L-histidine as substrate. kcat is 64 sec(-1) with D-histidine as substrate.


proof_lines: kcat is 502 sec(-1) with L-isoleucine as substrate. kcat is 939 sec(-1) with D-allo-isoleucine as substrate.

source_databases_merged: brenda uniprot


organism: Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)

substrate_name: L,L-lanthionine

proof_lines: kcat is 74 sec(-1) with L-histidine as substrate (PubMed:39424140). kcat is 250 sec(-1) with D-histidine as substrate (PubMed:39424140). kcat is 0.07 sec(-1) with L,L-lanthionine as substrate (PubMed:37329940).

substrate: L,L-lanthionine


organism: Leuconostoc mesenteroides subsp. sake


organism: Lactiplantibacillus plantarum

substrate_name: (R)-lactate

proof_lines: pH and temperature not specified in the publication

proof_lines: kcat is 4745 sec(-1) for conversion of L-lactate to D-lactate. kcat is 1333 sec(-1) for conversion of D-lactate to L-lactate.

substrate: (R)-lactate


organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer Tris-HCl

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I': Km = 15.51 mM, kcat = 1.82 s^(-1), kcat/Km = 117.82 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.51 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 15.51 mM. kcat: printed Table 2 cell 1.82 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.82 s^(-1). kcat/Km: printed Table 2 cell 117.82 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 117.82 / 1000 = 0.11782 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I: Km = 15.51 mM; kcat = 1.82 s^(-1); printed kcat/Km = 117.82 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I': Km = 15.10 mM, kcat = 2.60 s^(-1), kcat/Km = 172.25 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.10 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 15.1 mM. kcat: printed Table 2 cell 2.60 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.6 s^(-1). kcat/Km: printed Table 2 cell 172.25 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 172.25 / 1000 = 0.17225 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I: Km = 15.10 mM; kcat = 2.60 s^(-1); printed kcat/Km = 172.25 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I/Y54F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I/Y54F': Km = 14.52 mM, kcat = 2.57 s^(-1), kcat/Km = 176.70 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.52 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.52 mM. kcat: printed Table 2 cell 2.57 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.57 s^(-1). kcat/Km: printed Table 2 cell 176.70 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 176.70 / 1000 = 0.1767 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F: Km = 14.52 mM; kcat = 2.57 s^(-1); printed kcat/Km = 176.70 M^-1 s^-1.


sequence_variant_note: Mutation signature V22I/Y45F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V29I': Km = 11.99 mM, kcat = 1.45 s^(-1), kcat/Km = 121.37 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.99 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 11.99 mM. kcat: printed Table 2 cell 1.45 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.45 s^(-1). kcat/Km: printed Table 2 cell 121.37 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 121.37 / 1000 = 0.12137 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V29I: Km = 11.99 mM; kcat = 1.45 s^(-1); printed kcat/Km = 121.37 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V29I/Y45F with inferred residue-numbering offset -25 to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'WT': Km = 14.82 mM, kcat = 0.90 s^(-1), kcat/Km = 60.74 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.82 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.82 mM. kcat: printed Table 2 cell 0.90 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 0.9 s^(-1). kcat/Km: printed Table 2 cell 60.74 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60.74 / 1000 = 0.06074 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form WT: Km = 14.82 mM; kcat = 0.90 s^(-1); printed kcat/Km = 60.74 M^-1 s^-1.


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


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I': Km = 19.91 mM, kcat = 2.47 s^(-1), kcat/Km = 123.97 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 19.91 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 19.91 mM. kcat: printed Table 2 cell 2.47 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.47 s^(-1). kcat/Km: printed Table 2 cell 123.97 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 123.97 / 1000 = 0.12397 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I: Km = 19.91 mM; kcat = 2.47 s^(-1); printed kcat/Km = 123.97 M^-1 s^-1.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I': Km = 13.74 mM, kcat = 2.35 s^(-1), kcat/Km = 159.31 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 13.74 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 13.74 mM. kcat: printed Table 2 cell 2.35 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.35 s^(-1). kcat/Km: printed Table 2 cell 159.31 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 159.31 / 1000 = 0.15931 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I/V29I: Km = 13.74 mM; kcat = 2.35 s^(-1); printed kcat/Km = 159.31 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V29L 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_accession and applied mutation signature Y54A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54F with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54I with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54L with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54V with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


substrate_name: (R)-mandelamide

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26L to reconstruct the assayed variant sequence.

substrate: (R)-mandelamide


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V22I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L319F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V22L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26I/Y54I with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26I/Y54V with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


substrate_name: crotonyl-CoA (for enoyl-CoA hydratase activity)


substrate_name: acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)


substrate_name: NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)

assay_conditions_summary: cofactor NADH


enzyme_display_name: 4-hydroxyproline epimerase

organism: Streptosporangium roseum

column_label: Table 2 (PDF page 10 of 32); cluster 11; row group `Sros_6004 | D2AV87`; Function sub-row `4HypE`; columns kcat [s-1] = `14`, KM [mM] = `7.8`, kcat/KM[M-1s-1] = `1800`.

normalized_value_unit_evidence: kcat: printed cell 14 s^-1 -> 14.0 s^(-1); the export holds 14.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 7.8 mM -> 7.8 mM; the export holds 7.8 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 1800 M^-1 s^-1 converted as 1800 / 1000 = 1.8 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 1.794871794871795 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Sros_6004 | D2AV87`, sub-row `4HypE`: kcat = 14 s^-1; KM = 7.8 mM; kcat/KM = 1800 M^-1 s^-1.

row_label: Sros_6004 | D2AV87 / 4HypE (Table 2 cluster 11)

enzyme: 4-hydroxyproline epimerase


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


substrate_name: (R)-trifluorolactate

substrate: (R)-trifluorolactate


substrate_name: (S)-trifluorolactate

substrate: (S)-trifluorolactate


substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: D-allo-isoleucine

substrate: D-allo-isoleucine


substrate_name: (R)-mandelate

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

substrate: (R)-mandelate


substrate_name: (S)-Mandelate

substrate: (S)-Mandelate


substrate_name: Unknown


enzyme_display_name: serine racemase

organism: Oryza sativa

substrate_name: D-serine

proof_lines: mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication

proof_lines: mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

enzyme: serine racemase

substrate: D-serine


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

proof_lines: wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

proof_lines: wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication


enzyme_display_name: diaminopimelate epimerase

organism: Priestia megaterium

substrate_name: LL-diaminoheptanedioate

enzyme: diaminopimelate epimerase

substrate: LL-diaminoheptanedioate


substrate_name: meso-diaminoheptanedioate

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

substrate: meso-diaminoheptanedioate


enzyme_display_name: L-3-cyanoalanine synthase

organism: Pieris rapae

substrate_name: hydrogen sulfide

smiles: S

enzyme: L-3-cyanoalanine synthase

substrate: hydrogen sulfide


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: (R)-mandelamide


enzyme_display_name: methylmalonyl-CoA mutase

organism: Propionibacterium freudenreichii subsp. shermanii

enzyme: methylmalonyl-CoA mutase


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F


proof_lines: mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I/V29L


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L


proof_lines:
mutant V26L, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V26L
pH 7.5, 25°C, mutant V26L


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A


proof_lines:
mutant V29L, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V29L
pH 7.5, 25°C, mutant V29L


proof_lines:
mutant V22A, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+ mutant V22A
pH 7.5, 3.3 mM Mg2+, mutant V22A


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L


proof_lines: mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I


proof_lines: pH 7.5, mutant V22A, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V22F, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26F, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V29A, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26L, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26A, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V29F, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant T24S, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, wild-type, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V29L, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26A/V29L, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant A25V, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V22I, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V22I/V29L, addition of either 10 mM (R)- or (S)-mandelate


assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

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


substrate_name: adenosylcobalamin

substrate: adenosylcobalamin


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I/Y54F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I/Y54F': Km = 17.94 mM, kcat = 3.49 s^(-1), kcat/Km = 194.69 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 17.94 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 17.94 mM. kcat: printed Table 2 cell 3.49 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 3.49 s^(-1). kcat/Km: printed Table 2 cell 194.69 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 194.69 / 1000 = 0.19469 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F: Km = 17.94 mM; kcat = 3.49 s^(-1); printed kcat/Km = 194.69 M^-1 s^-1.


sequence_variant_note: Mutation signature V22I/Y45F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V29I': Km = 14.35 mM, kcat = 1.83 s^(-1), kcat/Km = 127.66 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.35 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.35 mM. kcat: printed Table 2 cell 1.83 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.83 s^(-1). kcat/Km: printed Table 2 cell 127.66 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 127.66 / 1000 = 0.12766 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V29I: Km = 14.35 mM; kcat = 1.83 s^(-1); printed kcat/Km = 127.66 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V29I/Y45F with inferred residue-numbering offset -25 to reconstruct the assayed variant sequence.


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

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'WT': Km = 17.74 mM, kcat = 0.99 s^(-1), kcat/Km = 56.34 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 17.74 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 17.74 mM. kcat: printed Table 2 cell 0.99 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 0.99 s^(-1). kcat/Km: printed Table 2 cell 56.34 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 56.34 / 1000 = 0.05634 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form WT: Km = 17.74 mM; kcat = 0.99 s^(-1); printed kcat/Km = 56.34 M^-1 s^-1.


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


organism: Pseudomonas aeruginosa

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: mutant H329A, pH 7.5, temperature not specified in the publication

substrate: alpha-D-glucose 1-phosphate


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


proof_lines:
25°C, pH 7.5, mutant enzyme N197A
mutant N197A

substrate: Unknown


substrate_name: methylglyoxal

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

substrate: methylglyoxal


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


enzyme_display_name: protoporphyrin ferrochelatase

enzyme: protoporphyrin ferrochelatase


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


proof_lines: 25°C, pH 7.5, mutant enzyme C92S/C264S/166thiaK


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


proof_lines:
mutant V29I, pH 7.5, 25°C
mutant V29I/V29I, 20 mM Mg2+, pH 7.5


proof_lines: mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+


enzyme_display_name: amino-acid racemase

substrate_name: D-Lys

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

enzyme: amino-acid racemase

substrate: D-Lys


substrate_name: D-Thr

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

substrate: D-Thr


substrate_name: L-Leu

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

substrate: L-Leu


substrate_name: (R)-mandelate


proof_lines:
mutant K166R
pH 7.5, 25°C, mutant enzyme K166R


enzyme_display_name: methionine gamma-lyase

organism: Pseudomonas sp.

enzyme: methionine gamma-lyase


substrate_name: L-methionine

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

substrate: L-methionine


enzyme_display_name: UniProt Q9A1H8

organism: Streptococcus pyogenes

substrate_name: D-ribulose 5-phosphate

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

enzyme: UniProt Q9A1H8

substrate: D-ribulose 5-phosphate


enzyme_display_name: UDP-glucose 4-epimerase

organism: Galdieria sulphuraria

substrate_name: UDPgalactose

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: UniProt A3MUJ4

organism: Pyrobaculum calidifontis

substrate_name: UDP-galactose

enzyme: UniProt A3MUJ4

substrate: UDP-galactose


enzyme_display_name: UniProt C8VAU8

organism: Aspergillus nidulans

substrate_name: UDP-alpha-D-glucose

enzyme: UniProt C8VAU8

substrate: UDP-alpha-D-glucose


enzyme_display_name: UniProt P09147

organism: Escherichia coli

substrate_name: D-galactose

enzyme: UniProt P09147

substrate: D-galactose


substrate_name: D-tagatose

substrate: D-tagatose


enzyme_display_name: guanylate cyclase

organism: Rattus norvegicus

substrate_name: GTP

proof_lines: pH 8.0, 30°C, wild-type enzyme, in presence of NO-donor S-nitroso-N-acetylpenicillamine

enzyme: guanylate cyclase

substrate: GTP


substrate_name: Unknown


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


substrate_name: kynurenine

substrate: kynurenine


enzyme_display_name: protein disulfide-isomerase

substrate_name: insulin-(SS)

enzyme: protein disulfide-isomerase

substrate: insulin-(SS)


substrate_name: GSH

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

substrate: GSH


enzyme_display_name: mandelate racemase

substrate_name: (S)-Mandelate

proof_lines:
mutant E317Q
E317Q mutant

enzyme: mandelate racemase

substrate: (S)-Mandelate


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


substrate: Unknown


enzyme_display_name: FAD-AMP lyase (cyclizing)

substrate_name: FAD

assay_conditions_summary: cofactor FAD

enzyme: FAD-AMP lyase (cyclizing)

substrate: FAD


enzyme_display_name: prostaglandin-D synthase

substrate_name: glutathione

proof_lines: conjugation of glutathione to 1-chloro-2,4-dinitrobenzene

enzyme: prostaglandin-D synthase

substrate: glutathione


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4 free acid

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4 free acid


substrate_name: leukotriene A4 methyl ester

substrate: leukotriene A4 methyl ester


organism: Poterioochromonas malhamensis


organism: Saccharomyces fragilis


enzyme_display_name: aldose 1-epimerase

organism: Batrachoididae gen. sp.

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


organism: Thermotoga maritima

substrate_name: UDP-alpha-D-galactose

proof_lines:
pH 7.0, 80°C
recombinant enzyme, pH 7.0, 80°C

substrate: UDP-alpha-D-galactose


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

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


organism: Meriones unguiculatus


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

proof_lines: mitochondria cytoplasm


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


organism: Capsicum frutescens


organism: Torulopsis candida

substrate_name: UDPgalactose

substrate: UDPgalactose


organism: Pyrococcus horikoshii


enzyme_display_name: L-ribulose-5-phosphate 4-epimerase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 20.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:9548961). kcat is 19.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:11732896). kcat is 17.3 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substr

enzyme: L-ribulose-5-phosphate 4-epimerase


substrate_name: L-ribulose 5-phosphate (LRu5P) (with zinc ion)


substrate_name: L-ribulose 5-phosphate (LRu5P)

proof_lines: kcat is 12 sec(-1) with L-ribulose 5-phosphate (LRu5P) as substrate.

substrate: L-ribulose 5-phosphate (LRu5P)


proof_lines: kcat is 25 sec(-1) with L-ribulose 5-phosphate (LRu5P) as substrate.


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Ovis aries

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

proof_lines: alpha-D-glucose, kidney, embryo and adult


organism: Perca flavescens


enzyme_display_name: tagaturonate epimerase

substrate_name: D-fructuronate

proof_lines: kcat is 6.5 sec(-1) with D-fructuronate as substrate.

enzyme: tagaturonate epimerase

substrate: D-fructuronate


enzyme_display_name: ribulose-phosphate 3-epimerase

organism: Oryza sativa subsp. japonica

substrate_name: Unknown

enzyme: ribulose-phosphate 3-epimerase


organism: Arabidopsis thaliana


organism: Homo sapiens


organism: Kluyveromyces marxianus


organism: Thermus thermophilus

assay_conditions_summary: pH 8.9; cofactor NAD+

proof_lines: recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase


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

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


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Escherichia coli

substrate_name: alpha-D-Galactose

substrate: alpha-D-Galactose


substrate_name: alpha-D-Glucose

substrate: alpha-D-Glucose


substrate_name: alpha-D-galactose

proof_lines: kcat is 12000 sec(-1) with galactose as substrate (PubMed:12753898). kcat is 4900 sec(-1) with glucose as substrate (PubMed:12753898).

substrate: alpha-D-galactose


normalized_value_unit_evidence: Normalized values: kcat=12000 s^-1; Km=37 mM; independently printed kcat/Km=340 s^-1 mM^-1 after converting 340000 L mol^-1 s^-1.

row_label: Galactose

table_label: Table 1. Kinetic parameters of human aldose 1-epimerase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H95N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08203 and applied mutation signature H97N to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'H97N', column 'CoCl2': Km = 1.67; kcat = 2.14; kcat/Km = 1.28.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.14 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 2.14 s^(-1). Km: printed Table 1 cell 1.67 in the Km cell of this cell group, whose head prints uM; 1.67 / 1000 = 0.00167 mM. kcat/Km: printed Table 1 cell 1.28 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.28 x 1000 = 1280.0 s^-1 mM^-1. Closure check on the paper's own cells: 2.14 / 0.00167 = 1281.437125748503 s^-1 mM^-1, which the printed efficiency cell 1.28 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'H97N', metal-ion column 'CoCl2': Km = 1.67 uM; kcat = 2.14 s^-1; printed kcat/Km = 1.28 uM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'CoCl2': Km = 0.29; kcat = 24.3; kcat/Km = 83.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 24.3 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 24.3 s^(-1). Km: printed Table 1 cell 0.29 in the Km cell of this cell group, whose head prints uM; 0.29 / 1000 = 0.00029 mM. kcat/Km: printed Table 1 cell 83.8 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 83.8 x 1000 = 83800.0 s^-1 mM^-1. Closure check on the paper's own cells: 24.3 / 0.00029 = 83793.10344827586 s^-1 mM^-1, which the printed efficiency cell 83.8 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'CoCl2': Km = 0.29 uM; kcat = 24.3 s^-1; printed kcat/Km = 83.8 uM^-1 s^-1.


substrate_name: L-Ribulose 5-phosphate

substrate: L-Ribulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H97N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08203 and applied mutation signature Y229F to reconstruct the assayed variant sequence.

column_label: Table 3 of Biochemistry 2000, volume 39, number 16, pages 4821-4830; the L-Ru5P kinetic constants table for the Zn(II)-substituted mutant enzymes, whose column groups print Km (mM), kcat (s^-1) and kcat/Km (mM^-1 s^-1). The metric is the printed row label and each column group prints Km (mM), kcat (s^-1) and kcat/Km (mM^-1 s^-1). Column group 'Zn(II)-Y229F': Km = 0.129; kcat = 0.0118; kcat/Km = 0.0915.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.0118 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 0.0118 s^(-1). Km: printed Table 3 cell 0.129 in the Km cell of this cell group, whose head prints mM, so no unit conversion applies and the paper value is 0.129 mM. kcat/Km: printed Table 3 cell 0.0915 in the kcat/Km cell of this cell group, whose head prints mM-1 s-1, the export unit, so no unit conversion applies and the printed cell is 0.0915 s^-1 mM^-1. Closure check on the paper's own cells: 0.0118 / 0.129 = 0.09147286821705426 s^-1 mM^-1, which the printed efficiency cell 0.0915 reproduces at the precision Table 3 uses.

raw_value_unit_evidence: Table 3, L-Ru5P column group 'Zn(II)-Y229F': Km = 0.129 mM; kcat = 0.0118 s^-1; printed kcat/Km = 0.0915 mM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'MgCl2': Km = 1350; kcat = 0.855; kcat/Km = 0.000633.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.855 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 0.855 s^(-1). Km: printed Table 1 cell 1350 in the Km cell of this cell group, whose head prints uM; 1350 / 1000 = 1.35 mM. kcat/Km: printed Table 1 cell 0.000633 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.000633 x 1000 = 0.633 s^-1 mM^-1. Quotient disclosure for this cell group: 0.855 / 1.35 = 0.6333333333333333 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell is that same quotient carried to the precision Table 1 uses, and it sits inside the last-place rounding interval of the quotient.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'MgCl2': Km = 1350 uM; kcat = 0.855 s^-1; printed kcat/Km = 0.000633 uM^-1 s^-1.


substrate_name: UDP-xylose

substrate: UDP-xylose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D103G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G319E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G90E with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K257R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L183P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L313M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N34S with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R335H with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V94M to reconstruct the assayed variant sequence.


organism: Hordeum vulgare

substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: UDP-D-glucose

substrate: UDP-D-glucose


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'MnCl2': Km = 0.54; kcat = 37.2; kcat/Km = 68.9.

normalized_value_unit_evidence: kcat: printed Table 1 cell 37.2 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 37.2 s^(-1). Km: printed Table 1 cell 0.54 in the Km cell of this cell group, whose head prints uM; 0.54 / 1000 = 0.00054 mM. kcat/Km: printed Table 1 cell 68.9 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 68.9 x 1000 = 68900.0 s^-1 mM^-1. Closure check on the paper's own cells: 37.2 / 0.00054 = 68888.88888888889 s^-1 mM^-1, which the printed efficiency cell 68.9 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'MnCl2': Km = 0.54 uM; kcat = 37.2 s^-1; printed kcat/Km = 68.9 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08203 and applied mutation signature H95N to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'H95N', column 'ZnCl2': Km = 2.02; kcat = 0.190; kcat/Km = 0.094.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.190 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 0.19 s^(-1). Km: printed Table 1 cell 2.02 in the Km cell of this cell group, whose head prints uM; 2.02 / 1000 = 0.00202 mM. kcat/Km: printed Table 1 cell 0.094 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.094 x 1000 = 94.0 s^-1 mM^-1. Closure check on the paper's own cells: 0.19 / 0.00202 = 94.05940594059406 s^-1 mM^-1, which the printed efficiency cell 0.094 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'H95N', metal-ion column 'ZnCl2': Km = 2.02 uM; kcat = 0.190 s^-1; printed kcat/Km = 0.094 uM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'H97N', column 'ZnCl2': Km = 0.53; kcat = 1.77; kcat/Km = 3.34.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.77 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 1.77 s^(-1). Km: printed Table 1 cell 0.53 in the Km cell of this cell group, whose head prints uM; 0.53 / 1000 = 0.00053 mM. kcat/Km: printed Table 1 cell 3.34 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 3.34 x 1000 = 3340.0 s^-1 mM^-1. Closure check on the paper's own cells: 1.77 / 0.00053 = 3339.622641509434 s^-1 mM^-1, which the printed efficiency cell 3.34 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'H97N', metal-ion column 'ZnCl2': Km = 0.53 uM; kcat = 1.77 s^-1; printed kcat/Km = 3.34 uM^-1 s^-1.


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

column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'ZnCl2': Km = 0.17; kcat = 16.7; kcat/Km = 98.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 16.7 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 16.7 s^(-1). Km: printed Table 1 cell 0.17 in the Km cell of this cell group, whose head prints uM; 0.17 / 1000 = 0.00017 mM. kcat/Km: printed Table 1 cell 98.2 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 98.2 x 1000 = 98200.0 s^-1 mM^-1. Closure check on the paper's own cells: 16.7 / 0.00017 = 98235.29411764706 s^-1 mM^-1, which the printed efficiency cell 98.2 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'ZnCl2': Km = 0.17 uM; kcat = 16.7 s^-1; printed kcat/Km = 98.2 uM^-1 s^-1.


organism: Pisum sativum

substrate_name: UDP-D-xylose

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NAD+

column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Xyl; column 'K m (mM)' = 0.15 ± 0.02; column 'k cat (s^-1)' = 17; column 'k cat/K m (mM^-1 s^-1)' = 115.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.15 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.15 mM; the exported value is 0.15 mM. kcat: printed Table 5 cell 17 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 17.0 s^(-1); the exported value is 17.0 s^(-1). kcat/Km: printed Table 5 cell 115 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 115.0 s^(-1)*mM^(-1); the exported value is 113.33333333333334 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Xyl: K m = 0.15 ± 0.02 mM; k cat = 17 s^-1; printed k cat/K m = 115 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Xyl

substrate: UDP-D-xylose


column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Gal; column 'K m (mM)' = 0.29 ± 0.03; column 'k cat (s^-1)' = 64; column 'k cat/K m (mM^-1 s^-1)' = 220.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.29 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.29 mM; the exported value is 0.29 mM. kcat: printed Table 5 cell 64 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 64.0 s^(-1); the exported value is 64.0 s^(-1). kcat/Km: printed Table 5 cell 220 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 220.0 s^(-1)*mM^(-1); the exported value is 220.6896551724138 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Gal: K m = 0.29 ± 0.03 mM; k cat = 64 s^-1; printed k cat/K m = 220 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Gal


substrate_name: UDP-glucose

column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Glc; column 'K m (mM)' = 0.31 ± 0.03; column 'k cat (s^-1)' = 9; column 'k cat/K m (mM^-1 s^-1)' = 28.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.31 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.31 mM; the exported value is 0.31 mM. kcat: printed Table 5 cell 9 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 9.0 s^(-1); the exported value is 9.0 s^(-1). kcat/Km: printed Table 5 cell 28 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 28.0 s^(-1)*mM^(-1); the exported value is 29.032258064516128 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Glc: K m = 0.31 ± 0.03 mM; k cat = 9 s^-1; printed k cat/K m = 28 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Glc

substrate: UDP-glucose


substrate_name: UDP-L-arabinose

column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Ara; column 'K m (mM)' = 0.16 ± 0.01; column 'k cat (s^-1)' = 23; column 'k cat/K m (mM^-1 s^-1)' = 141.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.16 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.16 mM; the exported value is 0.16 mM. kcat: printed Table 5 cell 23 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 23.0 s^(-1); the exported value is 23.0 s^(-1). kcat/Km: printed Table 5 cell 141 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 141.0 s^(-1)*mM^(-1); the exported value is 143.75 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Ara: K m = 0.16 ± 0.01 mM; k cat = 23 s^-1; printed k cat/K m = 141 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Ara

substrate: UDP-L-arabinose


organism: Spinacia oleracea

substrate_name: ribulose 5-phosphate

substrate: ribulose 5-phosphate


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Marinithermus hydrothermalis

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

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G118A/G119A with inferred residue-numbering offset -22 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G118S/G119S with inferred residue-numbering offset -22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S279Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S116A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T117S to reconstruct the assayed variant sequence.


organism: Aspergillus nidulans

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L320Y to reconstruct the assayed variant sequence.


substrate_name: UDP-galactose (at 37 degrees Celsius and pH 8.8)


substrate_name: UDPgalactose

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

proof_lines:
native and renatured enzyme
25°C, pH 8.8

substrate: UDPgalactose


assay_conditions_summary: pH 8.6; cofactor NAD+

proof_lines: recombinant enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase

proof_lines: recombinant enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase

proof_lines: recombinant enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDPGlc dehydrogenase

proof_lines: recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant enzyme UGE5, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase

proof_lines: recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


column_label: Table 6: Kinetics of rAtUGEs (Biochem. J. 2009, 424(2):169-177), UDP-Xyl block, enzyme row rAtUGE3; column 'K m (mM)' = 0.32 ± 0.05; column 'k cat (s^-1)' = 13; column 'k cat/K m (mM^-1 s^-1)' = 40.

normalized_value_unit_evidence: Km: printed Table 6 cell 0.32 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.32 mM; the exported value is 0.32 mM. kcat: printed Table 6 cell 13 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 13.0 s^(-1); the exported value is 13.0 s^(-1). kcat/Km: printed Table 6 cell 40 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 40.0 s^(-1)*mM^(-1); the exported value is 40.625 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 6, UDP-Xyl block, enzyme row rAtUGE3: K m = 0.32 ± 0.05 mM; k cat = 13 s^-1; printed k cat/K m = 40 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L320Y to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE1 fit. Columns read: kcatUDP-Gal (s^-1) cell 24 ⴞ 0.82, KmUDP-Gal (mM) cell 0.19 ⴞ 0.02, kUDP-Gal (mM^-1 s^-1) cell 126. metric: kcat; raw value: 24; raw unit: s^-1; normalized value: 24 s^(-1); metric: Km; raw value: 0.19; raw unit: mM; normalized value: 0.19 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 126.3157894736842 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE1 row of Table 4: kcat 24 s^-1 = 24 s^(-1) (no conversion); Km 0.19 mM stays 0.19 mM (table prints Km directly in mM); kcat/Km = 24 s^-1 / 0.19 mM = 126.3157894736842 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 126 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE1 row cells (quoted from extract line 347): 24 ⴞ 0.82          0.19 ⴞ 0.02         126         1.1        0.87 | cells read: kcat = 24 ⴞ 0.82 s^-1; Km = 0.19 ⴞ 0.02 mM; k = kcat Km^-1 = 126 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE1 | boldface highest-kcat fit (24 ⴞ 0.82)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE3 fit. Columns read: kcatUDP-Gal (s^-1) cell 66 ⴞ 1.7, KmUDP-Gal (mM) cell 0.22 ⴞ 0.021, kUDP-Gal (mM^-1 s^-1) cell 300. metric: kcat; raw value: 66; raw unit: s^-1; normalized value: 66 s^(-1); metric: Km; raw value: 0.22; raw unit: mM; normalized value: 0.22 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 300.0 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE3 row of Table 4: kcat 66 s^-1 = 66 s^(-1) (no conversion); Km 0.22 mM stays 0.22 mM (table prints Km directly in mM); printed catalytic efficiency k = 300 mM^-1 s^-1 = 300.0 s^-1 mM^-1 (mM^-1 s^-1 and s^-1 mM^-1 are the same unit), which equals the quotient 66/0.22 exactly. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE3 row cells (quoted from extract line 353): 66 ⴞ 1.7           0.22 ⴞ 0.021        300         0.64       0.94 | cells read: kcat = 66 ⴞ 1.7 s^-1; Km = 0.22 ⴞ 0.021 mM; k = kcat Km^-1 = 300 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE3 | boldface highest-kcat fit (66 ⴞ 1.7)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE4 fit. Columns read: kcatUDP-Gal (s^-1) cell 34 ⴞ 0.69, KmUDP-Gal (mM) cell 0.23 ⴞ 0.019, kUDP-Gal (mM^-1 s^-1) cell 148. metric: kcat; raw value: 34; raw unit: s^-1; normalized value: 34 s^(-1); metric: Km; raw value: 0.23; raw unit: mM; normalized value: 0.23 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 147.82608695652172 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE4 row of Table 4: kcat 34 s^-1 = 34 s^(-1) (no conversion); Km 0.23 mM stays 0.23 mM (table prints Km directly in mM); kcat/Km = 34 s^-1 / 0.23 mM = 147.82608695652172 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 148 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE4 row cells (quoted from extract line 356): 34 ⴞ 0.69          0.23 ⴞ 0.019        148         3.4        0.98 | cells read: kcat = 34 ⴞ 0.69 s^-1; Km = 0.23 ⴞ 0.019 mM; k = kcat Km^-1 = 148 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE4 | boldface highest-kcat fit (34 ⴞ 0.69)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE5 fit. Columns read: kcatUDP-Gal (s^-1) cell 128 ⴞ 3.86, KmUDP-Gal (mM) cell 0.17 ⴞ 0.026, kUDP-Gal (mM^-1 s^-1) cell 753. metric: kcat; raw value: 128; raw unit: s^-1; normalized value: 128 s^(-1); metric: Km; raw value: 0.17; raw unit: mM; normalized value: 0.17 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 752.9411764705882 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE5 row of Table 4: kcat 128 s^-1 = 128 s^(-1) (no conversion); Km 0.17 mM stays 0.17 mM (table prints Km directly in mM); kcat/Km = 128 s^-1 / 0.17 mM = 752.9411764705882 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 753 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE5 row cells (quoted from extract line 357): 5        128 ⴞ 3.86          0.17 ⴞ 0.026        753         0.14       0.92 | cells read: kcat = 128 ⴞ 3.86 s^-1; Km = 0.17 ⴞ 0.026 mM; k = kcat Km^-1 = 753 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE5 | boldface highest-kcat fit (128 ⴞ 3.86)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE2 fit. Columns read: kcatUDP-Gal (s^-1) cell 101 ⴞ 1.5, KmUDP-Gal (mM) cell 0.13 ⴞ 0.007, kUDP-Gal (mM^-1 s^-1) cell 777. metric: kcat; raw value: 101; raw unit: s^-1; normalized value: 101 s^(-1); metric: Km; raw value: 0.13; raw unit: mM; normalized value: 0.13 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 776.9230769230769 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE2 row of Table 4: kcat 101 s^-1 = 101 s^(-1) (no conversion); Km 0.13 mM stays 0.13 mM (table prints Km directly in mM); kcat/Km = 101 s^-1 / 0.13 mM = 776.9230769230769 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 777 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE2 row cells (quoted from extract line 350): 101 ⴞ 1.5           0.13 ⴞ 0.007        777         0.48       0.97 | cells read: kcat = 101 ⴞ 1.5 s^-1; Km = 0.13 ⴞ 0.007 mM; k = kcat Km^-1 = 777 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE2 | boldface highest-kcat fit (101 ⴞ 1.5)


substrate_name: UDPglucose

column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '1'; column 'kcat UDP-Glc' with unit 's-1' = 32; column 'Km UDP-Glc' with unit 'mM' = 0.76. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 32 s-1; already in s^-1, no unit conversion applies; the paper value is 32.0 s^(-1). Km: printed Table 5 cell 0.76 mM; already in mM, no unit conversion applies; the paper value is 0.76 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 42.10526315789474 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 32 / 0.76 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '1': kcat UDP-Glc = 32 s-1; Km UDP-Glc = 0.76 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 1

table_label: Table 5: Conversion of UDP-Glc by UGE isoforms (J. Biol. Chem. 2006, 281(25):17276-17285)

substrate: UDPglucose


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '3'; column 'kcat UDP-Glc' with unit 's-1' = 19; column 'Km UDP-Glc' with unit 'mM' = 0.19. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 19 s-1; already in s^-1, no unit conversion applies; the paper value is 19.0 s^(-1). Km: printed Table 5 cell 0.19 mM; already in mM, no unit conversion applies; the paper value is 0.19 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 100.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 19 / 0.19 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '3': kcat UDP-Glc = 19 s-1; Km UDP-Glc = 0.19 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 3


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '4'; column 'kcat UDP-Glc' with unit 's-1' = 28; column 'Km UDP-Glc' with unit 'mM' = 0.56. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 28 s-1; already in s^-1, no unit conversion applies; the paper value is 28.0 s^(-1). Km: printed Table 5 cell 0.56 mM; already in mM, no unit conversion applies; the paper value is 0.56 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 49.99999999999999 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 28 / 0.56 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '4': kcat UDP-Glc = 28 s-1; Km UDP-Glc = 0.56 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 4


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '5'; column 'kcat UDP-Glc' with unit 's-1' = 33; column 'Km UDP-Glc' with unit 'mM' = 0.13. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 33 s-1; already in s^-1, no unit conversion applies; the paper value is 33.0 s^(-1). Km: printed Table 5 cell 0.13 mM; already in mM, no unit conversion applies; the paper value is 0.13 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 253.84615384615384 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 33 / 0.13 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '5': kcat UDP-Glc = 33 s-1; Km UDP-Glc = 0.13 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 5


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '2'; column 'kcat UDP-Glc' with unit 's-1' = 24; column 'Km UDP-Glc' with unit 'mM' = 0.09. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 24 s-1; already in s^-1, no unit conversion applies; the paper value is 24.0 s^(-1). Km: printed Table 5 cell 0.09 mM; already in mM, no unit conversion applies; the paper value is 0.09 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 266.6666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 24 / 0.09 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '2': kcat UDP-Glc = 24 s-1; Km UDP-Glc = 0.09 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 2


organism: Saccharomyces cerevisiae

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


substrate_name: UDP-galactose

proof_lines: kcat is 760 sec(-1) for UDP-Glc (at pH 8.5 and 27 degrees Celsius) and 24 sec(-1) for UDP-Gal (at pH 8.5).

substrate: UDP-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D186A to reconstruct the assayed variant sequence.


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


sequence_variant_note: 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.


substrate_name: L-ribulose 5-phosphate

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

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H95N

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H95N

proof_lines: 22°C, pH 7.5, mutant enzyme H95N, activated by 0.1 mM ZnCl2

substrate: L-ribulose 5-phosphate


proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H97N

proof_lines: 22°C, pH 7.5, mutant enzyme H97N, activated by 0.1 mM ZnCl2

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H97N


proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme D76N

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme D76N


proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H97N or D76N


substrate_name: Unknown

proof_lines: 37°C, pH 7.6, mutant enzyme H97N, with L-ribulose 5-phosphate as substrate

substrate: Unknown


organism: Lactococcus lactis

substrate_name: alpha-D-xylose

substrate: alpha-D-xylose


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


substrate_name: alpha-L-arabinose

substrate: alpha-L-arabinose


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


substrate_name: alpha-D-Glucose

column_label: Table 1, row/column Glucose, metric rows Km/mM, kcat/s^-1, and (kcat/Km)/l mol^-1 s^-1; PDF page 2 / article page 22

normalized_value_unit_evidence: Km normalized_value=54 normalized_unit=mM; kcat normalized_value=4900 normalized_unit=s^-1; kcat_over_km normalized_value=90 normalized_unit=s^-1*mM^-1

row_label: Glucose

substrate: alpha-D-Glucose


proof_lines: pH 6.2, temperature not specified in the publication, recombinant mutant Y149F


proof_lines: pH 6.2, temperature not specified in the publication, recombinant mutant S124A


proof_lines: pH 6.2, temperature not specified in the publication, recombinant S124T


proof_lines: pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme


organism: Aeromonas hydrophila

assay_conditions_summary: pH 8; 298.15 K; buffer 20 mM sodium phosphate

proof_lines: mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C


proof_lines: mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C


proof_lines: wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C


organism: Thermotoga maritima

substrate_name: D-fructuronate

substrate: D-fructuronate


organism: Rattus norvegicus

substrate_name: alpha-D-Fucose

proof_lines: alpha-D-xylose, enzyme form II from kidney and liver

substrate: alpha-D-Fucose


proof_lines: alpha-D-xylose, enzyme form I and II from small intestine

proof_lines: enzyme form III from kidney, enzyme form I and II from small intestine


proof_lines:
enzyme form IV from liver
enzyme form IV from kidney


substrate_name: D-fucose

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

proof_lines: alpha-D-galactose, enzyme form IV from liver

proof_lines: beta-L-arabinose, enzyme form III from kidney

substrate: D-fucose


substrate_name: beta-D-arabinose

substrate: beta-D-arabinose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: lactose

substrate: lactose


proof_lines: wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C

proof_lines: wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C


organism: Bos taurus


substrate_name: alpha-D-quinovose

substrate: alpha-D-quinovose


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Campylobacter jejuni


proof_lines: 22°C, pH 7.5, mutant enzyme Y229F, activated by 0.1 mM ZnCl2


proof_lines: 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MgCl2

proof_lines: 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM ZnCl2


organism: Streptococcus pyogenes

substrate_name: D-ribulose 5-phosphate

proof_lines: RPE metal-free, stoichiometry of Zn2+: 0.1 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate

proof_lines: RPE as isolated, stoichiometry of Zn2+: 0.3 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate

proof_lines: RPE as isolated + 0.5 mM ZnCl2 present in assay, stoichiometry of Zn2+: 0.9 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Lathyrus oleraceus

proof_lines: 50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme


substrate_name: UDP-xylose

substrate: UDP-xylose


substrate_name: L-cystathionine

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

assay_conditions_summary: pH 8.5; 310.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C

substrate: L-cystathionine


substrate_name: L-djenkolate

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

substrate: L-djenkolate


enzyme_display_name: cellobiose epimerase

organism: Thermoanaerobacterium saccharolyticum

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


organism: Caldicellulosiruptor saccharolyticus

substrate_name: epilactose

substrate: epilactose


organism: Dictyoglomus turgidum


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E161D/N365P with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E161D/S180P/S351G to reconstruct the assayed variant sequence.


substrate_name: lactulose

substrate: lactulose


organism: Escherichia coli

substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-tagatose

substrate: D-tagatose


substrate_name: UDP-galactose

substrate: UDP-galactose


substrate_name: L-ribulose 5-phosphate

substrate: L-ribulose 5-phosphate


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: myoglobin

enzyme: protoporphyrin ferrochelatase

substrate: myoglobin


organism: Ricinus communis

proof_lines:
2-phosphoglycerate, cytosolic enzyme
plastidic enzyme


proof_lines:
cytosolic enzyme
plastidic enzyme


organism: Cellvibrio vulgaris

substrate_name: D-mannose

substrate: D-mannose


substrate_name: lactose

proof_lines:
pH 8.0, 40°C, recombinant enzyme
pH 7.5, 30°C, recombinant enzyme

substrate: lactose


enzyme_display_name: UDP-arabinose 4-epimerase

organism: Sinorhizobium meliloti

substrate_name: UDP-D-xylopyranose

proof_lines: apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6

enzyme: UDP-arabinose 4-epimerase

substrate: UDP-D-xylopyranose


substrate_name: UDP-alpha-D-xylopyranose

substrate: UDP-alpha-D-xylopyranose


enzyme_display_name: UDP-N-acetylglucosamine 4-epimerase

substrate_name: UDP-D-glucose

enzyme: UDP-N-acetylglucosamine 4-epimerase

substrate: UDP-D-glucose


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Geotrichum fermentans

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: lactoylglutathione lyase

organism: Saccharomyces cerevisiae

substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: the apparent kinetic parameters are determined by varying the hemithioacetal concentration between 0.3 and 1.5 mM, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal

enzyme: lactoylglutathione lyase

substrate: methylglyoxal


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


enzyme_display_name: D-tagatose 3-epimerase

organism: Sinorhizobium sp.

substrate_name: D-sorbose

protein_accession_database: NCBI Protein

sequence_source: NCBI RefSeq protein WP_069063284.1

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

column_label: Table-wrap tab1 captioned kinetic parameters of sDTE wild-type on four substrates lists the D-Sorbose row with Km 83 +/- 4.3 mM, kcat 34.0 +/- 0.92 s^-1, and kcat/Km 0.41 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=83.0 normalized_unit=mM; kcat normalized_value=34.0 normalized_unit=s^-1; kcat/Km paper_cell=0.41 normalized_unit=s^-1 mM^-1; CatLog stores computed 34.0/83.0=0.40963855421686746

raw_value_unit_evidence: Km raw_value=83 +/- 4.3 raw_unit=mM; kcat raw_value=34.0 +/- 0.92 raw_unit=s^-1; kcat/Km raw_value=0.41 raw_unit=s^-1 mM^-1

row_label: D-Sorbose row

table_label: PMC9059984 full-text table-wrap tab1

enzyme: D-tagatose 3-epimerase

substrate: D-sorbose


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: methylmalonyl-CoA mutase

substrate_name: adenosylcobalamin

proof_lines:
37°C, pH 7, in presence of 3 mM NH4+
37°C, pH 7, without NH4+

enzyme: methylmalonyl-CoA mutase

substrate: adenosylcobalamin


substrate_name: (R,S)-methylmalonyl-CoA

substrate: (R,S)-methylmalonyl-CoA


organism: Hordeum vulgare


organism: Triticum aestivum

substrate_name: UDP-L-arabinose

substrate: UDP-L-arabinose


organism: Thermothelomyces thermophilus

substrate_name: cellobiose

substrate: cellobiose


organism: Helianthus tuberosus

substrate_name: UDP-D-xylose

substrate: UDP-D-xylose


organism: Marinithermus hydrothermalis

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

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


enzyme_display_name: UDP-glucuronate 4-epimerase

organism: Dolichospermum flos-aquae

substrate_name: UDPglucuronate

enzyme: UDP-glucuronate 4-epimerase

substrate: UDPglucuronate


organism: Bacillus cereus

substrate_name: UDP-glucuronate

substrate: UDP-glucuronate


organism: Giardia duodenalis

substrate_name: UDP-N-acetylglucosamine

proof_lines:
Vmax 1.02 mM/min
Vmax 0.59 mM/min

substrate: UDP-N-acetylglucosamine


enzyme_display_name: N-acylglucosamine 2-epimerase

organism: Synechocystis sp.

substrate_name: N-acetyl-D-mannosamine

enzyme: N-acylglucosamine 2-epimerase

substrate: N-acetyl-D-mannosamine


organism: Thermotoga maritima

substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


proof_lines:
pH 7.0, 80°C
recombinant enzyme, pH 7.0, 80°C


organism: Badhamia polycephala


organism: Caldicellulosiruptor saccharolyticus

substrate_name: lactose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371A to reconstruct the assayed variant sequence.

substrate: lactose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W355Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W355A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E174D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N175K/G176D with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G176D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E174H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E174A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I178D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V177D with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G176K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R170A/F171A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N175K to reconstruct the assayed variant sequence.


organism: Methanococcus maripaludis

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

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

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


organism: Anabaena sp. CH1

substrate_name: N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E242Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: E242Q, reverse conversion in the presence of 1 mM ATP

substrate: N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R375K to reconstruct the assayed variant sequence.

proof_lines: R375K, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E218D to reconstruct the assayed variant sequence.

proof_lines: E218D, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R375A to reconstruct the assayed variant sequence.

proof_lines: R375A, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E218A to reconstruct the assayed variant sequence.

proof_lines: E218A, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C370A to reconstruct the assayed variant sequence.

proof_lines: C370A, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N179A to reconstruct the assayed variant sequence.

proof_lines: N179A, reverse conversion in the presence of 1 mM ATP


organism: Arabidopsis thaliana

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

proof_lines: recominant Arabidopsis thaliana enzyme UGE3, 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: kcat is 19 sec(-1) with UDP-glucose as substrate (PubMed:16644739). kcat is 42 sec(-1) with UDP-galactose as substrate (PubMed:16644739). kcat is 57 sec(-1) with UDP-galactose as substrate (PubMed:16644739). kcat is 66 sec(-1) with UDP-gala


proof_lines: recombinant Arabidopsis thaliana enzyme UGE1, 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)


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

proof_lines: pH 7.5, 70°C, mutant enzyme RaC (CsCE_loop168-178 is replaced by RaCE_loop164-174)

proof_lines: pH 7.5, 70°C, mutant enzyme RmC (CsCE_loop168-178 is replaced by RmCE_loop180-190)

proof_lines: pH 7.5, 70°C, mutant enzyme Bt (CsCE_loop168-178 is replaced by BtCE_loop168-178)


organism: Caldicellulosiruptor obsidiansis

proof_lines: pH and temperature not specified in the publication

proof_lines: recombinant His6-tagged enzyme, pH 7.5, 70°C


organism: Dictyoglomus turgidum (strain DSM 6724 / Z-1310)

proof_lines: kcat is 169 min(-1) with cellobiose as substrate. kcat is 89.4 min(-1) with lactose as substrate.


substrate_name: lactulose

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

substrate: lactulose