organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.


organism: Dictyostelium discoideum

substrate_name: UDP-Gal

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: The catalytic efficiency with the presumed natural substrate Fuc-alpha-1,2-Gal-beta-1,3-GlcNAc-alpha-1-Skp1 is 21-fold and 21000-fold higher than that of the synthetic substrates Fuc-alpha-1,2-Gal-beta-1-pNP and Fuc-alpha-1-Bn, respectively

substrate: UDP-Gal

source: uniprot


organism: Homo sapiens

substrate_name: type I H-antigen (A transferase)

proof_lines: kcat is 1.3 sec(-1) for type I H-antigen (A transferase) (PubMed:16326711). kcat is 0.5 sec(-1) for type I H-antigen (B transferase) (PubMed:16326711). kcat is 1.8 sec(-1) for type II H-antigen (A transferase) (PubMed:16326711). kcat is 1.2

substrate: type I H-antigen (A transferase)


enzyme_display_name: cytidine deaminase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: cytidine

proof_lines: kcat is 4.8 and 3.5 sec(-1) with cytidine and 2-deoxycytidine as substrate, respectively.

enzyme: cytidine deaminase

substrate: cytidine


enzyme_display_name: low-specificity L-threonine aldolase

organism: Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)

substrate_name: L-serine (at pH 7.5 and 70 degrees Celsius)

proof_lines: kcat is 18.7 sec(-1) for the L-serine hydroxymethyltransferase reaction, 2.3 sec(-1) for the L-threonine cleavage, and 18.0 sec(-1) for the L-allo-threonine cleavage, at 70 degrees Celsius. In the THF-independent aldolase reaction, the rate

enzyme: low-specificity L-threonine aldolase


organism: Mycobacterium tuberculosis

substrate_name: alpha-D-glucosamine 1-phosphate

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProt direct accession lookup: A5U161 / GLMU_MYCTA

data_origin: experimental

substrate: alpha-D-glucosamine 1-phosphate

status: unverified

source: oed


substrate_name: acetyl-CoA

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProt direct accession lookup: P9WMN2 / GLMU_MYCTO

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA

source: skid


organism: Sulfurisphaera tokodaii

source_db: brenda

sequence_source: UniProt direct accession lookup: Q975F9 / S1PNA_SULTO

assay_conditions_summary: pH 7.5; 353.15 K; cofactor CoA

source: brenda


substrate_name: alpha-D-galactosamine 1-phosphate

mutation_signature: deletion mutant D011 of ST0452 protein

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

mutation_type: deletion

proof_lines: pH 7.5, 80°C, deletion mutant D011 of ST0452 protein

substrate: alpha-D-galactosamine 1-phosphate


mutation_signature: deletion mutant D005 of ST0452 protein

proof_lines: pH 7.5, 80°C, deletion mutant D005 of ST0452 protein


sequence_source: Reconstructed from UniProt Q975F9 canonical sequence using selected note: DC011 deletion of the C-terminal 11 residues of ST0452

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein


proof_lines:
pH 7.5, 80°C, wild-type ST0452 protein
pH 7.5, 80°C, wild-type enzyme


sequence_source: Reconstructed from UniProt Q975F9 canonical sequence using selected note: DC005 deletion of the C-terminal 5 residues of ST0452

proof_lines: pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein


organism: Yersinia pestis

sequence_source: UniProt direct accession lookup: Q8Z9S7 / GLMU_YERPE

assay_conditions_summary: pH 8.2; 310.15 K; cofactor CoA


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


mutation_type: substitution


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


enzyme_display_name: 4-hydroxyacetophenone monooxygenase

organism: Pseudomonas fluorescens

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

proof_lines:
pH 7.5, 30°C
pH 8, 30°C
pH 7.5, 30°C, pH-dependent

enzyme: 4-hydroxyacetophenone monooxygenase


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: above, pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, R339A mutant

substrate: NADPH


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439F mutant


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439A mutant


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439N mutant


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439P mutant


substrate_name: NADH

proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, wild-type HAPMO

substrate: NADH


organism: Pseudomonas putida

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: pH 8, 30°C, 4-hydroxyacetophenone as substrate


enzyme_display_name: dopamine beta-monooxygenase

organism: Bos taurus

proof_lines:
5 mM tyramine
in presence of tyramine
pH 6.0, 28°C, 1.0 mM tyramine

enzyme: dopamine beta-monooxygenase


organism: Drosophila melanogaster

substrate_name: tyramine

proof_lines: at 10 mM ascorbate, 0.058 mM O2, pH 6 and 35°C

proof_lines: at 50 mM ascorbate, 1.04 mM O2, pH 6 and 35°C

substrate: tyramine


organism: Felis catus

substrate_name: ascorbate

proof_lines:
with or without Cu2+
in the absence of Cu2+
in the presence of Cu2+

substrate: ascorbate


organism: Gallus gallus

substrate_name: dopamine

substrate: dopamine


organism: Escherichia coli (strain K12)

substrate_name: N-acetylglucosamine 1-phosphate

substrate: N-acetylglucosamine 1-phosphate


substrate_name: GlcNAc-1-P (at pH 7.6)

assay_conditions_summary: pH 7.6; cofactor CoA

substrate: GlcNAc-1-P (at pH 7.6)


organism: Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1)

substrate_name: phosphate

substrate: phosphate


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


organism: Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)

substrate_name: diphosphate

substrate: diphosphate


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


organism: Treponema pallidum (strain DSM 117211 / Nichols)


organism: Winmispira thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1)


organism: Xanthomonas campestris pv. campestris (strain B100)


organism: Homo sapiens


organism: Mus musculus

substrate_name: pNppp (isoform 1)

substrate: pNppp (isoform 1)


enzyme_display_name: uracil-DNA glycosylase

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: uracil-DNA glycosylase

substrate: ATP


organism: Escherichia coli

substrate_name: D-Glucosamine 1-phosphate

sequence_source: direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P0ACC7.json

substrate: D-Glucosamine 1-phosphate


substrate_name: D-Glucosamine 1-phosphate; Acetyl-CoA

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

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU C324A N-terminal His6-tagged

substrate: D-Glucosamine 1-phosphate; Acetyl-CoA


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ACC7 and applied mutation signature C385A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 310.15 K; buffer 20 mM potassium phosphate; cofactor CoA

column_label: Table 1 (page 4800), decoded plain-numeral transcription, row 'His6-GlmU C385A': column 'Km (mM) GlcN-1-P' = 0.2; column 'kcat (s^-1) Acetyltransferase' = 1,450. Table 1 prints no kcat/Km column for any row.

normalized_value_unit_evidence: Km: printed cell 0.2 in the column 'Km (mM) GlcN-1-P', so the printed unit is mM and no unit conversion applies; the exported km is 0.2 mM. kcat: printed cell 1,450 in the column 'kcat (s^-1) Acetyltransferase', so the printed unit is s^-1 and no unit conversion applies; the exported kcat is 1450.0 s^(-1). kcat/Km: Table 1 prints no kcat/Km column, so the exported kcat_over_km is the same-measurement quotient of this row's own two printed cells, 1,450 / 0.2 = 7250.0 s^(-1)*mM^(-1), which is the exported value.

raw_value_unit_evidence: Table 1 (decoded plain-numeral transcription), row 'His6-GlmU C385A': column 'Km (mM) GlcN-1-P' = 0.2; column 'kcat (s^-1) Acetyltransferase' = 1,450. Table 1 prints no kcat/Km column.

row_label: Table 1, row 'His6-GlmU C385A', catalog substrate GlcN-1-P

table_label: TABLE 1. Kinetic parameters of wild-type and mutant GlmU enzymes

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ACC7 and applied mutation signature C324A to reconstruct the assayed variant sequence.

column_label: Table 1 (page 4800), decoded plain-numeral transcription, row 'His6-GlmU C324A': column 'Km (mM) GlcN-1-P' = 0.12; column 'kcat (s^-1) Acetyltransferase' = 160. Table 1 prints no kcat/Km column for any row.

normalized_value_unit_evidence: Km: printed cell 0.12 in the column 'Km (mM) GlcN-1-P', so the printed unit is mM and no unit conversion applies; the exported km is 0.12 mM. kcat: printed cell 160 in the column 'kcat (s^-1) Acetyltransferase', so the printed unit is s^-1 and no unit conversion applies; the exported kcat is 160.0 s^(-1). kcat/Km: Table 1 prints no kcat/Km column, so the exported kcat_over_km is the same-measurement quotient of this row's own two printed cells, 160 / 0.12 = 1333.3333333333335 s^(-1)*mM^(-1), which is the exported value.

raw_value_unit_evidence: Table 1 (decoded plain-numeral transcription), row 'His6-GlmU C324A': column 'Km (mM) GlcN-1-P' = 0.12; column 'kcat (s^-1) Acetyltransferase' = 160. Table 1 prints no kcat/Km column.

row_label: Table 1, row 'His6-GlmU C324A', catalog substrate GlcN-1-P


substrate_name: Acetyl-CoA; D-Glucosamine 1-phosphate

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU C296A N-terminal His6-tagged

substrate: Acetyl-CoA; D-Glucosamine 1-phosphate


organism: Mycobacterium tuberculosis

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

sequence_source: direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines:
pH 7.5, 37°C, recombinant enzyme
Raw SKiD Env: Temp=30°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json and applied mutation signature N397A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json and applied mutation signature H374A to reconstruct the assayed variant sequence.


substrate_name: alpha-D-glucosamine 1-phosphate

sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json and applied mutation signature S416A to reconstruct the assayed variant sequence.

substrate: alpha-D-glucosamine 1-phosphate


substrate_name: propionyl-CoA

sequence_source: direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/A5U161.json

assay_conditions_summary: pH 7.5; 303.15 K; buffer containing 10 mM MgCl2 throughout the purification process; cofactor CoA

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'Pro-CoA', fixed-substrate column value 'GlcN-1P'; column 'K_m (uM)' = 60; column 'k_cat (s^-1)' = 0.5; column 'k_cat/K_m (M^-1 s^-1)' = 8.3 x 10^3; column 'K_d (uM)' = 500 uM.

normalized_value_unit_evidence: Km: printed Table 1 cell 60 uM; 60 / 1000 = 0.06 mM. kcat: printed Table 1 cell 0.5 s^-1; already in s^-1, no unit conversion applies, so the paper value is 0.5 s^(-1). kcat/Km: printed Table 1 cell 8.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.3 x 10^3 / 1000 = 8.3 s^-1 mM^-1. The catalog carries 8.333333333333334 s^(-1)*mM^(-1) for this metric, which is the exact quotient 0.5 / 0.06 of the same table line's printed kcat and Km cells; the printed efficiency cell reproduces that quotient at the two-significant-figure precision the paper uses, so the exact quotient is kept.

raw_value_unit_evidence: Table 1, varied-substrate row 'Pro-CoA', fixed substrate 'GlcN-1P': Km = 60 uM; kcat = 0.5 s^-1; printed kcat/Km = 8.3 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate-analogue row with varied substrate 'Pro-CoA' and fixed substrate 'GlcN-1P'

table_label: Table 1: Steady-State Kinetic Parameters for GlmU (Biochemistry 2018, 57, 3387-3401)

substrate: propionyl-CoA


substrate_name: acetoacetyl-CoA

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines:
pH 7.5, 30°C
cosubstrate propionyl-CoA, pH 7.5, 30°C
cosubstrate acetyl-CoA, pH 7.5, 30°C

source_databases_merged: brenda skid

substrate: acetoacetyl-CoA


column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'AAc-CoA', fixed-substrate column value 'GlcN-1P'; column 'K_m (uM)' = 1800; column 'k_cat (s^-1)' = 0.5; column 'k_cat/K_m (M^-1 s^-1)' = 2.8 x 10^2; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 1800 uM; 1800 / 1000 = 1.8 mM. kcat: printed Table 1 cell 0.5 s^-1; already in s^-1, no unit conversion applies, so the paper value is 0.5 s^(-1). kcat/Km: printed Table 1 cell 2.8 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^2 / 1000 = 0.28 s^-1 mM^-1. The catalog carries 0.2777777777777778 s^(-1)*mM^(-1) for this metric, which is the exact quotient 0.5 / 1.8 of the same table line's printed kcat and Km cells; the printed efficiency cell reproduces that quotient at the two-significant-figure precision the paper uses, so the exact quotient is kept.

raw_value_unit_evidence: Table 1, varied-substrate row 'AAc-CoA', fixed substrate 'GlcN-1P': Km = 1800 uM; kcat = 0.5 s^-1; printed kcat/Km = 2.8 x 10^2 M^-1 s^-1.

row_label: Table 1, substrate-analogue row with varied substrate 'AAc-CoA' and fixed substrate 'GlcN-1P'


substrate_name: succinyl-CoA

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'Suc-CoA', fixed-substrate column value 'GlcN-1P'; column 'K_m (uM)' = 1100; column 'k_cat (s^-1)' = 0.9; column 'k_cat/K_m (M^-1 s^-1)' = 8.2 x 10^2; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 1100 uM; 1100 / 1000 = 1.1 mM. kcat: printed Table 1 cell 0.9 s^-1; already in s^-1, no unit conversion applies, so the paper value is 0.9 s^(-1). kcat/Km: printed Table 1 cell 8.2 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.2 x 10^2 / 1000 = 0.82 s^-1 mM^-1. The catalog carries 0.8181818181818181 s^(-1)*mM^(-1) for this metric, which is the exact quotient 0.9 / 1.1 of the same table line's printed kcat and Km cells; the printed efficiency cell reproduces that quotient at the two-significant-figure precision the paper uses, so the exact quotient is kept.

raw_value_unit_evidence: Table 1, varied-substrate row 'Suc-CoA', fixed substrate 'GlcN-1P': Km = 1100 uM; kcat = 0.9 s^-1; printed kcat/Km = 8.2 x 10^2 M^-1 s^-1.

row_label: Table 1, substrate-analogue row with varied substrate 'Suc-CoA' and fixed substrate 'GlcN-1P'

substrate: succinyl-CoA


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


enzyme_display_name: chitosanase

organism: Aspergillus fumigatus

enzyme: chitosanase


organism: Bacillus amyloliquefaciens

substrate_name: chitosan

km_display: Not reported

substrate: chitosan


organism: Bacillus cereus


organism: Bacillus sp.

substrate_name: H2O; Chitosan

unit: lgwedgeoneswedgeone

substrate: H2O; Chitosan


organism: Bacillus sp. MN


substrate_name: chitopentaose

substrate: chitopentaose


organism: Bacillus subtilis


substrate_name: dUMP-carrying ssDNA and dsDNA

substrate: dUMP-carrying ssDNA and dsDNA


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: G/U dsDNA

substrate: G/U dsDNA


organism: Arabidopsis thaliana

substrate_name: cytidine (at pH 7.5 and 37 degrees Celsius)


substrate_name: L-threonine

substrate: L-threonine


enzyme_display_name: homoserine dehydrogenase

organism: Mycobacterium leprae

substrate_name: Unknown

ki_unit: mM

proof_lines: pH and temperature not specified in the publication

enzyme: homoserine dehydrogenase

substrate: Unknown


organism: Pyrococcus horikoshii

substrate_name: NADP+

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58802 and applied mutation signature K57A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 323.15 K; cofactor NADP+

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'K57A', NADP header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.06; column 'kcat s-1' = 26.7; column 'kcat/Km s-1 mM-1' = 518.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.06 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.06 mM. kcat: printed Table 2 cell 26.7 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 26.7 s^(-1). kcat/Km: printed Table 2 cell 518 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 518.0 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'K57A', NADP header block: Km = 0.06 mM; kcat = 26.7 s-1; printed kcat/Km = 518 s-1 mM-1.

table_label: Table 2: kinetic parameters for the NAD and NADP coenzyme blocks (Scientific Reports 2015, volume 5, article 11674)

substrate: NADP+

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:O58802 and applied mutation signature R40A to reconstruct the assayed variant sequence.


substrate_name: NAD+

assay_conditions_summary: pH 9; 323.15 K; cofactor NAD+

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'Wild type', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.32; column 'kcat s-1' = 70.1; column 'kcat/Km s-1 mM-1' = 219.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.32 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.32 mM. kcat: printed Table 2 cell 70.1 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 70.1 s^(-1). kcat/Km: printed Table 2 cell 219 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the printed cell normalizes to 219.0 s^(-1)*mM^(-1); the catalog carries the full-precision quotient of the same two printed cells, 70.1 / 0.32 = 219.0625 s^(-1)*mM^(-1), which the printed cell renders at integer precision.

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', NAD header block: Km = 0.32 mM; kcat = 70.1 s-1; printed kcat/Km = 219 s-1 mM-1.

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from UniProtKB:O58802 and applied mutation signature K57A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58802 and applied mutation signature R40A to reconstruct the assayed variant sequence.

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'R40A', NADP header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.04; column 'kcat s-1' = 3.4; column 'kcat/Km s-1 mM-1' = 89.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.04 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.04 mM. kcat: printed Table 2 cell 3.4 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 3.4 s^(-1). kcat/Km: printed Table 2 cell 89.1 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 89.1 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'R40A', NADP header block: Km = 0.04 mM; kcat = 3.4 s-1; printed kcat/Km = 89.1 s-1 mM-1.


column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'K57A', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.05; column 'kcat s-1' = 48.5; column 'kcat/Km s-1 mM-1' = 1020.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.05 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.05 mM. kcat: printed Table 2 cell 48.5 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 48.5 s^(-1). kcat/Km: printed Table 2 cell 1020 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 1020.0 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'K57A', NAD header block: Km = 0.05 mM; kcat = 48.5 s-1; printed kcat/Km = 1020 s-1 mM-1.


column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'R40A', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.95; column 'kcat s-1' = 96.1; column 'kcat/Km s-1 mM-1' = 102.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.95 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.95 mM. kcat: printed Table 2 cell 96.1 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 96.1 s^(-1). kcat/Km: printed Table 2 cell 102 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 102.0 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'R40A', NAD header block: Km = 0.95 mM; kcat = 96.1 s-1; printed kcat/Km = 102 s-1 mM-1.


proof_lines: pH 9.0, 50°C, recombinant wild-type enzyme


substrate_name: L-homoserine

proof_lines:
pH 9.0, 50°C, recombinant enzyme
Raw SKiD Env: Temp=50°C, pH=9

substrate: L-homoserine


organism: Saccharomyces cerevisiae

substrate_name: L-Aspartate 4-semialdehyde

column_label: Retained supplementary PDF Supplementary Table 2, Sc-Hom6 natural-substrate row: kcat 126 +/- 23; Km 0.22 +/- 0.04; kcat/Km 573.

normalized_value_unit_evidence: At retained catalog units, kcat is 126 s^-1, Km is 0.22 mM, and the independently printed kcat/Km is 573 s^-1 mM^-1.

raw_value_unit_evidence: Supplementary Table 2 Sc-Hom6 natural-substrate row: kcat 126 +/- 23 s^-1; Km 0.22 +/- 0.04 mM; independently printed kcat/Km 573 s^-1 mM^-1.

row_label: Sc-Hom6 / Natural substrate

table_label: Supplementary Table 2. Kinetic parameters of wild-type homoserine pathway enzymes on their natural substrates and the corresponding intermediates of the synthetic DHB pathway

substrate: L-Aspartate 4-semialdehyde


substrate_name: H+; L-Aspartate 4-semialdehyde; NADPH

assay_conditions_summary: cofactor NADP+

substrate: H+; L-Aspartate 4-semialdehyde; NADPH


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines:
pH 8.0, 30°C, oxidized enzyme
pH 8.0, 30°C, reduced enzyme
pH 8.0, 30°C


organism: Thermotoga maritima

assay_conditions_summary: pH 10.5; 328.15 K; cofactor NADP+


organism: Thermus thermophilus

assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+


proof_lines: pH 9.5, 50°C, recombinant enzyme, with NAD+


substrate_name: L-Aspartate 4-semialdehyde; H+; NADPH; L-Aspartate 4-semialdehyde; H+; ...

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

sequence_source: UniProtKB:O81852 direct accession sequence

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines: pH 8.0, 37°C, purified recombinant soluble enzyme


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


substrate_name: NADP+; L-Homoserine; NADP+; L-Homoserine; ...

sequence_variant_note: Resolved canonical sequence from UniProtKB:O81852 canonical sequence with Q443A reconstruction and applied mutation signature Q443A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: homoserine dehydrogenase(Enzyme) mutant Q443A


substrate_name: L-Homoserine; NADP+; L-Homoserine; NADP+; ...

sequence_variant_note: Resolved canonical sequence from UniProtKB:O81852 canonical sequence with Q524A reconstruction and applied mutation signature Q524A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: homoserine dehydrogenase(Enzyme) mutant Q524A


column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2), RESULTS, 'Comparison of AK-HSDH Isoform Kinetic Properties': RESULTS prose pair for HSDH II: Km for aspartate semialdehyde 311 +/- 6 uM; catalytic constant 196 +/- 21 s^-1: kcat (catalytic constant v/[E]0) = 196 +/- 21 s^-1; Km = 311 +/- 6 uM.

normalized_value_unit_evidence: Printed catalytic constant 196 +/- 21 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 196.0. Printed Km 311 +/- 6 uM / 1000 = 0.311 mM, matching the catalog km 0.311 mM exactly. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 630.225080385852 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 196.0 / 0.311 = 630.225080385852.

raw_value_unit_evidence: RESULTS prose pair for HSDH II: Km for aspartate semialdehyde 311 +/- 6 uM; catalytic constant 196 +/- 21 s^-1: printed kcat (catalytic constant v/[E]0) 196 +/- 21 s^-1; printed Km 311 +/- 6 uM; no printed kcat/Km.

table_label: RESULTS prose, 'Comparison of AK-HSDH Isoform Kinetic Properties' (no numbered table; values printed in the running text)


sequence_source: UniProtKB:Q9SA18 direct accession sequence

column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2), RESULTS, 'Comparison of AK-HSDH Isoform Kinetic Properties': RESULTS prose pair for HSDH I: Km for aspartate semialdehyde 290 +/- 17 uM; catalytic constant 245 +/- 19 s^-1: kcat (catalytic constant v/[E]0) = 245 +/- 19 s^-1; Km = 290 +/- 17 uM.

normalized_value_unit_evidence: Printed catalytic constant 245 +/- 19 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 245.0. Printed Km 290 +/- 17 uM / 1000 = 0.29 mM, matching the catalog km 0.29 mM exactly. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 844.8275862068966 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 245.0 / 0.29 = 844.8275862068966.

raw_value_unit_evidence: RESULTS prose pair for HSDH I: Km for aspartate semialdehyde 290 +/- 17 uM; catalytic constant 245 +/- 19 s^-1: printed kcat (catalytic constant v/[E]0) 245 +/- 19 s^-1; printed Km 290 +/- 17 uM; no printed kcat/Km.


assay_conditions_summary: cofactor NADPH

substrate: L-Aspartate 4-semialdehyde; H+; NADPH; L-Aspartate 4-semialdehyde; H+; ...


sequence_source: UniProtKB:P19582 direct accession sequence

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


substrate_name: NADP+; L-homoserine

substrate: NADP+; L-homoserine


substrate_name: L-Homoserine

substrate: L-Homoserine


organism: Escherichia coli

sequence_source: UniProtKB:P00561 direct accession sequence

substrate: L-Homoserine; NADP+; L-Homoserine; NADP+; ...


organism: Glycine max

substrate_name: L-homoserine; L-aspartate 4-semialdehyde; NADH; ...

sequence_source: UniProtKB:O65027 direct accession sequence

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines:
cosubstrate NAD+, pH 8.0, 25°C
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NADH, pH 8.0, 25°C


sequence_source: UniProtKB:O63067 direct accession sequence

proof_lines:
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C
cosubstrate NADH, pH 8.0, 25°C

substrate: L-homoserine; L-aspartate 4-semialdehyde; NADH; ...


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


substrate_name: L-aspartate 4-semialdehyde; L-homoserine; NADPH; ...

sequence_source: UniProtKB:Q3S3F6 direct accession sequence

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 8.0, 25°C
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C


organism: Hordeum vulgare

proof_lines:
isozyme I
isozyme II


organism: Lathyrus oleraceus

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines:
threonine sensitive isozyme
isozyme II
threonine insensitive isozyme


organism: Triticum aestivum

substrate_name: NADPH

proof_lines:
threonine sensitive isozyme
threonine resistant isozyme

substrate: NADPH


organism: Zea mays

proof_lines: threonine-sensitive enzyme, pH and temperature not specified in the publication


organism: Unknown

substrate_name: beta-glycinamide ribonucleotide

substrate: beta-glycinamide ribonucleotide


sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/Q5SL04.json

assay_conditions_summary: pH 9.5; 323.15 K; cofactor NAD+


sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/P08179.json


organism: Homo sapiens

sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/P22102.json

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


organism: Mus musculus

sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/Q64737.json


enzyme_display_name: acylaminoacyl-peptidase

organism: Aeropyrum pernix

substrate_name: p-nitrophenyl caprylate

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526K to reconstruct the assayed variant sequence.

enzyme: acylaminoacyl-peptidase

substrate: p-nitrophenyl caprylate


substrate_name: N-acetyl-Leu-p-nitroanilide

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526A to reconstruct the assayed variant sequence.

substrate: N-acetyl-Leu-p-nitroanilide


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526I to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/Q9YBQ2.json

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

proof_lines:
80°C, wild-type enzyme
pH 7.0, 70°C, wild-type enzyme
wild-type


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature H367A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature D524N to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 70°C, mutant enzyme D524N, measured under first-order conditions


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature D524A to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json)


proof_lines: pH 7.0, 70°C, mutant enzyme D524A, measured under first-order conditions


sequence_source: UniProtKB:Q9YBQ2 direct REST lookup


organism: Aeropyrum pernix K1

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature H367A and applied mutation signature H367A to reconstruct the assayed variant sequence.

proof_lines:
mutant H367A, larger than 0.1
mutant H367A


substrate_name: Ac-Leu-p-nitroanilide

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature D15A/R18A and applied mutation signature D15A/R18A to reconstruct the assayed variant sequence.

substrate: Ac-Leu-p-nitroanilide


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature R18A and applied mutation signature R18A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature ΔN21 could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature D15A and applied mutation signature D15A to reconstruct the assayed variant sequence.


proof_lines: wild-type, in the presence of 1 M sodium chloride


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature E88A/R526V and applied mutation signature E88A/R526V to reconstruct the assayed variant sequence.

proof_lines: mutant E88A/R526V, in the presence of 1 M sodium chloride


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature E88A and applied mutation signature E88A to reconstruct the assayed variant sequence.

proof_lines: mutant E88A, in the presence of 1 M sodium chloride


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature R526V and applied mutation signature R526V to reconstruct the assayed variant sequence.

proof_lines: mutant R526V, in the presence of 1 M sodium chloride


organism: Arabidopsis thaliana

substrate_name: N-acetyl-Ala-p-nitroanilide

sequence_source: UniProtKB:Q84LM4 direct REST lookup

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

substrate: N-acetyl-Ala-p-nitroanilide


organism: Bombyx mori

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

proof_lines:
pH 7.5, 25°C, recombinant enzyme
pH 7.5, 45°C, recombinant enzyme


organism: Saccharolobus solfataricus

substrate_name: N-acetyl-L-leucyl 4-nitroanilide

sequence_source: UniProtKB:Q7LX61 direct REST lookup

substrate: N-acetyl-L-leucyl 4-nitroanilide


proof_lines: pH 7.5, 80°C, substrate: N-acetyl-L-leucyl 4-nitroanilide


substrate_name: N-acetyl-L-alanyl 4-nitroanilide

substrate: N-acetyl-L-alanyl 4-nitroanilide


sequence_source: UniProtKB Q97VD6 direct REST lookup


proof_lines: in 25 mM Tris-HCl buffer pH 7.5, at 90°C

proof_lines: pH 7.5, 90°C, substrate: acetyl-Leu-4-nitroanilide


organism: Trematomus bernacchii

sequence_source: UniProtKB V5QZ74 direct REST lookup

proof_lines:
15°C, pH 8
50°C, pH 8
37°C, pH 8


substrate_name: Ac-Ala-pNA

assay_conditions_summary: pH 7

substrate: Ac-Ala-pNA


organism: Escherichia coli (strain K12)

proof_lines: kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5).


organism: Rattus norvegicus

substrate_name: N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine (f-MLF) (at pH 7)

proof_lines: kcat is 4.6 sec(-1) with N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine (f-MLF) as substrate (at pH 7). kcat is 14 sec(-1) with N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine (f-MLF) as substrate (at pH 8). kcat is 5.6 sec(-1) w


mutation_signature: deletion construct with amino acids 68-354 / donor UDP-GalNAc deletion construct with amino acids 68-354

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

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc


mutation_signature: deletion construct with amino acids 68-354 / co-substrate: donor UDP-GalNAc deletion construct with amino acids 68-354

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc


proof_lines: mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose

proof_lines: mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc

proof_lines: mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc


organism: Oryctolagus cuniculus

substrate_name: UDP-galactose

proof_lines:
in reaction with N-acetyllactosamine
in reaction with 2-fucosyllactose

substrate: UDP-galactose


enzyme_display_name: non-specific protein-tyrosine kinase

proof_lines: pH 8.0, 30°C, recombinant mutant E338A Csk

enzyme: non-specific protein-tyrosine kinase


proof_lines: pH 8.0, 30°C, recombinant Csk residue-339-deletion mutant


substrate_name: [kdSrc kinase]-L-tyrosine

proof_lines: pH 8.0, 30°C, recombinant mutant R281A/R283A

substrate: [kdSrc kinase]-L-tyrosine


proof_lines: pH 8.0, 30°C, recombinant mutant S280A/R281A/R283A/F381A


proof_lines: pH 8.0, 30°C, recombinant W188A Csk mutant


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, recombinant DSH3 Csk mutant

proof_lines: pH 8.0, 30°C, recombinant DSH2 Csk mutant


proof_lines: pH 8.0, 30°C, recombinant K361G/K362A Csk mutant


proof_lines: pH 8.0, 30°C, recombinant W188F Csk mutant


substrate_name: tyramine

proof_lines: enzyme from serum of 27-weeks-old rats, at 37°C, pH not specified in the publication

proof_lines: enzyme from serum of 15-weeks-old rats, at 37°C, pH not specified in the publication

proof_lines: enzyme from serum of 8-weeks-old rats, at 37°C, pH not specified in the publication

substrate: tyramine


organism: Escherichia coli

substrate_name: NADP+; L-Homoserine

proof_lines: recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity

proof_lines: recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity

proof_lines: recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity

substrate: NADP+; L-Homoserine


substrate_name: L-homoserine

proof_lines: recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity

substrate: L-homoserine


organism: Spinacia oleracea

substrate_name: DL-aspartate 4-semialdehyde

assay_conditions_summary: cofactor NADH

substrate: DL-aspartate 4-semialdehyde


proof_lines:
mutant 13N + 13C 1:1
mutant B13


proof_lines:
pH 7.5
pH 8.5
purT gene product


proof_lines:
mutant H108A
strain H108A


organism: Yersinia pseudotuberculosis

substrate_name: alpha-D-glucosamine 1-phosphate

assay_conditions_summary: pH 8.2; 310.15 K; cofactor CoA

proof_lines: pH 8.2, 37°C, recombinant His6-tagged enzyme

substrate: alpha-D-glucosamine 1-phosphate


organism: Dictyostelium discoideum


substrate_name: UDP-N-acetylgalactosamine

proof_lines: with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor

substrate: UDP-N-acetylgalactosamine


substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: UDP-Gal

substrate: UDP-Gal


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


mutation_signature: deletion construct with amino acids 68-354 / co-substrate: donor UDP-alpha-D-galactose deletion construct with amino acids 68-354

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose


mutation_signature: deletion construct with amino acids 68-354 / donor UDP-alpha-D-galactose deletion construct with amino acids 68-354

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, donor UDP-alpha-D-galactose


substrate_name: UDP-GalNAc

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication

substrate: UDP-GalNAc


proof_lines: mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc

proof_lines: mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose

proof_lines: mutant C80S/C196S, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08179 plus direct D144A reconstruction and applied mutation signature D144A to reconstruct the assayed variant sequence.

proof_lines:
mutant D144A
strain D144A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08179 plus direct N106G reconstruction and applied mutation signature N106G to reconstruct the assayed variant sequence.


organism: Gallus gallus


substrate_name: beta-glycinamide ribonucleotide

proof_lines: chimeric enzyme GPX-M55 (hGART1-56/PurN58-212)

proof_lines: chimeric enzyme GPX-M24 (hGART1-54/PurN55-212)

proof_lines: chimeric enzyme GPG-N11 (hGART1-56/PurN57-131/hGART132-202)

substrate: beta-glycinamide ribonucleotide


proof_lines:
wild type enzyme
wild-type enzyme


substrate_name: N-acetyl-D-glucosamine 1-phosphate

sequence_source: UniProtKB:P0ACC7 canonical wild-type sequence

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

assay_conditions_summary: cofactor CoA

proof_lines:
GmlU uridyltransferase
uridyltransferase activity

substrate: N-acetyl-D-glucosamine 1-phosphate


substrate_name: D-glucosamine 1-phosphate

substrate: D-glucosamine 1-phosphate


substrate_name: acetyl-CoA

proof_lines: mutant His6GlmU, mutant His6-GlmU C296A, mutant His6-GlmU C385A

substrate: acetyl-CoA


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
pH 7.5, 25°C
pH 7.5, 37°C
Vmax: 4.489 microM/min/pmol enzyme


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A


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


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A


organism: Yersinia pestis


organism: Homo sapiens

substrate_name: EEEEY

substrate: EEEEY


substrate_name: ATP

proof_lines: pH 8.0, 30°C, recombinant mutant H384Q/Y416F

substrate: ATP


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


proof_lines: pH 8.0, 30°C, recombinant mutant H384Y/Y527F


proof_lines: pH 8.0, 30°C, recombinant mutant H384Y/Y416F


assay_conditions_summary: cofactor ATP

proof_lines: recombinant GST-fusion Chk, 12 mM Mg2+, no Mn2+

proof_lines: non-receptor tyrosine kinase Src, pH and temperature not specified in the publication


organism: Monosiga brevicollis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Acholeplasma laidlawii

substrate_name: Diphosphate; D-Fructose 6-phosphate

substrate: Diphosphate; D-Fructose 6-phosphate


organism: Ananas comosus

substrate_name: D-fructose 1,6-bisphosphate

proof_lines: pH 7.7, 25°C, in presence of fructose 2,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Brassica nigra

proof_lines: pH 6.8, 25°C, in presence of fructose 2,6-bisphosphate


organism: Bacillus subtilis

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


sequence_variant_note: Mutation signature K133A matches the mutant residue at offset +0 and the reference residue at offset +6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature R140A matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature R134A matches the mutant residue at offset +0 and the reference residue at offset +6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: adenine2085 in 23S rRNA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature R134A to reconstruct the assayed variant sequence.

substrate: adenine2085 in 23S rRNA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature M196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature N192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature K197A/N200A/E202A/K204A/K205A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature K197A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature T108A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature R140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature F163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed F163A single substitution and applied mutation signature F163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed K168A single substitution and applied mutation signature K168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed N11A single substitution and applied mutation signature N11A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed N11A single substitution


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed E128A single substitution and applied mutation signature E128A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed E128A single substitution


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed K166A single substitution and applied mutation signature K166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed P165A single substitution and applied mutation signature P165A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed K168A single substitution


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed K166A single substitution


sequence_source: UniProt P13956 reviewed canonical 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 P13956 canonical sequence with reviewer-reconstructed N101A single substitution and applied mutation signature N101A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed N101A single substitution


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed P165A single substitution


substrate_name: 23S rRNA; S-Adenosyl-L-methionine

proof_lines: pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA

substrate: 23S rRNA; S-Adenosyl-L-methionine


organism: Streptomyces fradiae

substrate_name: S-Adenosyl-L-methionine; rRNA

sequence_source: UniProt P45439 reviewed canonical sequence

substrate: S-Adenosyl-L-methionine; rRNA


enzyme_display_name: arylsulfatase (type I)

organism: Clostridium perfringens

substrate_name: 4-Nitrophenyl sulfate; H2O

sequence_source: UniProtKB REST direct accession lookup for Q0TUK6

enzyme: arylsulfatase (type I)

substrate: 4-Nitrophenyl sulfate; H2O


substrate_name: 4-Nitrocatechol sulfate; H2O

sequence_source: UniProtKB REST direct accession lookup for Q96EG1

substrate: 4-Nitrocatechol sulfate; H2O


substrate_name: 4-nitrocatechol sulfate

sequence_source: UniProtKB REST direct accession lookup for Q6UWY0

substrate: 4-nitrocatechol sulfate


substrate_name: Unknown

sequence_source: UniProtKB REST direct accession lookup for Q8IWU6

substrate: Unknown


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


organism: Marinomonas sp. FW-1

substrate_name: 4-nitrophenyl sulfate

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

substrate: 4-nitrophenyl sulfate


organism: Pseudoalteromonas atlantica


organism: Pseudoalteromonas carrageenovora

sequence_source: UniProtKB REST direct accession lookup for P28607


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for P28607 plus row mutation reconstruction and applied mutation signature H260L to reconstruct the assayed variant sequence.


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

proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260F


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260I


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260Q


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260R


proof_lines: 55°C, pH not specified in the publication, wild-type enzyme


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260L


organism: Bruguiera sexangula

substrate_name: D-fructose 6-phosphate

proof_lines:
pH 7.2, 30°C
pH 7.2, 30°C, presence of 0.15 mM NaCl

substrate: D-fructose 6-phosphate


organism: Citrus sinensis

assay_conditions_summary: pH 7.2; 298.15 K; buffer + NaCl, pH 7

proof_lines: forward reaction, HEPES-NaOH buffer + NaCl, pH 7.2, 25°C

proof_lines: forward reaction, Tris-HCl buffer, pH 7.2, 25°C


organism: Clostridium thermosuccinogenes


organism: Daucus carota

proof_lines:
forward reaction, pH 8.0, 25°C
reverse reaction, pH 8.0, 25°C
pH 8.0, 25°C


organism: Dictyoglomus thermophilum


organism: Entamoeba histolytica

substrate_name: diphosphate

proof_lines:
wild-type, pH 7.2, 30°C
wild-type enzyme, pH 7.2, 30°C

substrate: diphosphate


substrate_name: D-Fructose 6-phosphate; Diphosphate

proof_lines:
37°C, pH 7.0
forward reaction, pH 7.0, 30°C
pH 7.0, 30°C

substrate: D-Fructose 6-phosphate; Diphosphate


organism: Giardia duodenalis

substrate_name: phosphate

proof_lines: substrate is a Mg2+-chelated complexe of phosphate, not uncomplexed ligand

substrate: phosphate


organism: Glycine max

proof_lines:
pH 7.5, 25°C
with diphosphate


organism: Pseudomonas aeruginosa

substrate_name: testosterone 17-sulfate

sequence_source: UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta

substrate: testosterone 17-sulfate


substrate_name: etiocholanolonesulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/A323D/L325F/K330V/W358Y to reconstruct the assayed variant sequence.

substrate: etiocholanolonesulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/P161A/L325F/K330V


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/I156V/P161A/A323D/L325F/K330V/W358N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/I156V/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/I156V/L325F/K330V


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/P329R/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/P161A/P329R/L325F/K330V


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/A323Q/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/P161A/A323Q/L325F/K330V


enzyme_display_name: aqualysin 1

organism: Thermus aquaticus

sequence_source: UniProtKB direct accession lookup P08594 (SV=2); https://rest.uniprot.org/uniprotkb/P08594.fasta

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

enzyme: aqualysin 1


column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row Wild-type; column 'k cat (s -1 )' = 91.6 ± 2.75; column 'K m (mM)' = 0.79 ± 0.04; column 'k cat / K m (mM -1 s -1 )' = 116.

normalized_value_unit_evidence: kcat: printed Table 3 cell 91.6 ± 2.75 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 91.6 s^(-1). Km: printed Table 3 cell 0.79 ± 0.04 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.79 mM. kcat/Km: printed Table 3 cell 116 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 116.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row Wild-type: k_cat = 91.6 ± 2.75 s^-1; K_m = 0.79 ± 0.04 mM; printed k_cat/K_m = 116 mM^-1 s^-1.

row_label: Table 3, enzyme row Wild-type

table_label: Table 3: Kinetic parameters of the wild-type and mutant enzymes (AMB Express 2014, 4:59)


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D138N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D138N; column 'k cat (s -1 )' = 59.5 ± 6.14; column 'K m (mM)' = 0.77 ± 0.01; column 'k cat / K m (mM -1 s -1 )' = 77.3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 59.5 ± 6.14 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 59.5 s^(-1). Km: printed Table 3 cell 0.77 ± 0.01 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.77 mM. kcat/Km: printed Table 3 cell 77.3 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 77.3 s^-1 mM^-1.

row_label: Table 3, enzyme row D138N


organism: Hexamita inflata


organism: Methylococcus capsulatus

proof_lines: using D-fructose 6-phosphate as cosubstrate, in 0.1 M HEPES-HCl, pH 7.0, at 30°C

proof_lines: using D-fructose 1,6-bisphosphate as cosubstrate, in 0.1 M HEPES-HCl, pH 7.0, at 30°C


organism: Methylosinus trichosporium


organism: Methylotuvimicrobium alcaliphilum

proof_lines: in 50 mM Tris-HCl, pH 7.5, 5 mM MgCl2, at 30°C


organism: Musa acuminata


organism: Musa cavendishii

proof_lines: pH 7.0, 25°C, presence of 0.005 mM D-fructose 1,6-diphosphate


organism: Naegleria fowleri


organism: Oryza sativa

proof_lines: versus fructose 6-phosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration

proof_lines: versus diphosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration


organism: Phaseolus coccineus


organism: Phaseolus vulgaris


organism: Propionibacterium freudenreichii

proof_lines:
reverse reaction, pH 8.0, 25°C
as Mg2+ complex, pH 8.0, 25°C
pH 8.0, 25°C


organism: Propionibacterium freudenreichii subsp. shermanii

proof_lines:
pH 7.4, 25°C
pH 8.0, 25°C
forward reaction, pH 8.0, 25°C


organism: Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)

substrate_name: para-nitrophenyl sulfate

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

substrate: para-nitrophenyl sulfate


organism: Homo sapiens

substrate_name: p-nitrocatechol sulfate

substrate: p-nitrocatechol sulfate


organism: Azotobacter vinelandii

substrate_name: NAD+; 4-Methylthio-2-oxobutanoate; Coenzyme A

assay_conditions_summary: cofactor NAD+


substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


organism: Corynebacterium glutamicum

substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

proof_lines: SABIO-RK modifier species: Enzyme mutant AceF K162Q-K278Q

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

proof_lines: SABIO-RK modifier species: Enzyme mutant AceF K43Q-K162Q

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


organism: Escherichia coli

substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


organism: Rattus norvegicus


organism: Solanum tuberosum

substrate_name: 2-Oxoglutarate; Coenzyme A; NAD+

substrate: 2-Oxoglutarate; Coenzyme A; NAD+


organism: Sus scrofa


organism: Xenopus laevis


organism: Yarrowia lipolytica

substrate_name: DL-dihydrolipoamide

substrate: DL-dihydrolipoamide


enzyme_display_name: aliphatic nitrilase

organism: Rhodococcus rhodochrous

substrate_name: m-tolunitrile

sequence_source: UniProtKB:Q03217 direct FASTA lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03217 direct FASTA lookup and applied mutation signature K9A to reconstruct the assayed variant sequence.

enzyme: aliphatic nitrilase

substrate: m-tolunitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03217 direct FASTA lookup and applied mutation signature Y142F to reconstruct the assayed variant sequence.


substrate_name: Benzonitrile

substrate: Benzonitrile


organism: Synechocystis sp.

sequence_source: UniProtKB:Q55949 direct FASTA lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 direct FASTA lookup and applied mutation signature W146H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 direct FASTA lookup and applied mutation signature W146Y to reconstruct the assayed variant sequence.


substrate_name: Fumaronitrile

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

smiles: N#C/C=C/C#N

substrate: Fumaronitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 direct FASTA lookup and applied mutation signature W146F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature D423del to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D423DEL, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature D423A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature D423G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419del to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H419DEL, at pH 8.0 and 30°C


enzyme_display_name: ribonuclease P

organism: Arabidopsis thaliana

substrate_name: H2O; tRNA precursor

enzyme: ribonuclease P

substrate: H2O; tRNA precursor


substrate_name: pre-tRNA-Cys

proof_lines:
25°C, pH 7.8
presence of theophylline, pH 7.6, 37°C
pH 7.6, 37°C

substrate: pre-tRNA-Cys


organism: Bacillus subtilis


organism: Methanococcus maripaludis

substrate_name: pre-tRNATyr

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

proof_lines:
37°C, pH 7.5, in the absence of L7Ae
37°C, pH 7.5, in the presence of L7Ae

substrate: pre-tRNATyr


organism: Thermotoga maritima

substrate_name: pre-tRNAPhe

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature K53A to reconstruct the assayed variant sequence.

substrate: pre-tRNAPhe


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature R59A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature K62A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature R89A to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant R89A/U52C, pH 7.5, 37°C


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


substrate_name: tRNA(Gln) precursor

substrate: tRNA(Gln) precursor


organism: Thermus aquaticus

sequence_source: UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature G61D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D17N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D17N; column 'k cat (s -1 )' = 110 ± 4.48; column 'K m (mM)' = 0.98 ± 0.05; column 'k cat / K m (mM -1 s -1 )' = 113.

normalized_value_unit_evidence: kcat: printed Table 3 cell 110 ± 4.48 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 110.0 s^(-1). Km: printed Table 3 cell 0.98 ± 0.05 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.98 mM. kcat/Km: printed Table 3 cell 113 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 113.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row D17N: k_cat = 110 ± 4.48 s^-1; K_m = 0.98 ± 0.05 mM; printed k_cat/K_m = 113 mM^-1 s^-1.

row_label: Table 3, enzyme row D17N


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D183N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D183N; column 'k cat (s -1 )' = 53.0 ± 3.03; column 'K m (mM)' = 0.74 ± 0.05; column 'k cat / K m (mM -1 s -1 )' = 71.6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 53.0 ± 3.03 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 53.0 s^(-1). Km: printed Table 3 cell 0.74 ± 0.05 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.74 mM. kcat/Km: printed Table 3 cell 71.6 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 71.6 s^-1 mM^-1.

row_label: Table 3, enzyme row D183N


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature E237Q with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature S277D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature D138N matches the mutant residue at offset +11 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D58N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D58N; column 'k cat (s -1 )' = 68.5 ± 1.37; column 'K m (mM)' = 0.99 ± 0.07; column 'k cat / K m (mM -1 s -1 )' = 70.0.

normalized_value_unit_evidence: kcat: printed Table 3 cell 68.5 ± 1.37 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 68.5 s^(-1). Km: printed Table 3 cell 0.99 ± 0.07 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.99 mM. kcat/Km: printed Table 3 cell 70.0 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 70.0 s^-1 mM^-1.

row_label: Table 3, enzyme row D58N


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature D212N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


organism: Cereibacter sphaeroides


organism: Fusarium proliferatum

sequence_source: UniProt:A0A0E3D8K7 exact accession lookup; REST checked 2026-06-17 UTC

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


organism: Pseudomonas fluorescens

substrate_name: sebaconitrile

sequence_source: UniProt:Q4KCL8 exact accession lookup; REST checked 2026-06-17 UTC

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

substrate: sebaconitrile


sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature Y142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature Y142S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature Y142V to reconstruct the assayed variant sequence.


substrate_name: adiponitrile

sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature L79A to reconstruct the assayed variant sequence.

substrate: adiponitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed W146F substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature W146F to reconstruct the assayed variant sequence.

smiles: C/C=C/C#N


sequence_source: UniProtKB:Q55949 canonical sequence with reconstructed W146F substitution(s); RCSB 3WUY maps the structure entity to Q55949.


sequence_source: UniProtKB:Q55949 canonical sequence; RCSB 3WUY maps the structure entity to Q55949.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed W146Y substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature W146Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q55949 canonical sequence with reconstructed W146Y substitution(s); RCSB 3WUY maps the structure entity to Q55949.


organism: Synechocystis sp. PCC 6803

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed V198L substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature V198L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed W170G substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature W170G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed V198L/W170G substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature V198L/W170G to reconstruct the assayed variant sequence.


substrate_name: Succinonitrile

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

proof_lines: pH 7.5, temperature not specified in the publication

substrate: Succinonitrile


organism: uncultured bacterium

substrate_name: glutaronitrile

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

proof_lines: at 30°C in 50 mM sodium phosphate buffer (pH 7.5) and 1 mM dithiothreitol

substrate: glutaronitrile


organism: Aquifex aeolicus (strain VF5)

substrate_name: pre-tRNA(Gly)

substrate: pre-tRNA(Gly)


organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)

substrate_name: pre-tRNA-Tyr in the absence of L7Ae

proof_lines: kcat 10 min(-1) in absence of L7Ae, 63 min(-1) in presence of L7Ae. Kinetic parameters determined at 37 degrees Celsius.

substrate: pre-tRNA-Tyr in the absence of L7Ae


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: E.coli pre-tRNA(Tyr)

proof_lines: kcat is 9.5 min(-1). For enzyme reconstituted with RNA and 4 known subunits (Rnp1-4).

substrate: E.coli pre-tRNA(Tyr)


organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

substrate_name: phenylacetonitrile

proof_lines: kcat is 111 min(-1) with phenylacetonitrile.

substrate: phenylacetonitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature K56A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature F21A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA

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


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA checked as protein context only

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA checked as canonical protein context

proof_lines: recombinant mutant F17A/U52C, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R15A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA checked; variant not reconstructed


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R14A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature K90A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature K51A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R65A to reconstruct the assayed variant sequence.


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature G262D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row G262D; column 'k cat (s -1 )' = 61.3 ± 1.86; column 'K m (mM)' = 0.93 ± 0.15; column 'k cat / K m (mM -1 s -1 )' = 66.2.

normalized_value_unit_evidence: kcat: printed Table 3 cell 61.3 ± 1.86 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 61.3 s^(-1). Km: printed Table 3 cell 0.93 ± 0.15 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.93 mM. kcat/Km: printed Table 3 cell 66.2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 66.2 s^-1 mM^-1.

row_label: Table 3, enzyme row G262D


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature S277D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row S277D; column 'k cat (s -1 )' = 73.6 ± 5.51; column 'K m (mM)' = 0.80 ± 0.12; column 'k cat / K m (mM -1 s -1 )' = 92.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 73.6 ± 5.51 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 73.6 s^(-1). Km: printed Table 3 cell 0.80 ± 0.12 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.8 mM. kcat/Km: printed Table 3 cell 92.5 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 92.5 s^-1 mM^-1.

row_label: Table 3, enzyme row S277D


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08594 FASTA; variant reconstructed using UniProt mature-chain offset +127 and applied mutation signature D58N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: SupS1 precursor

proof_lines: in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin

substrate: SupS1 precursor


organism: Methanocaldococcus jannaschii

substrate_name: tRNA precursor

proof_lines: pH 8.0, 65°C, in presence of 800 mM ammonium acetate and 5 mM MgCl2

substrate: tRNA precursor


organism: Methanothermobacter thermautotrophicus

proof_lines: pH 8.0, 50°C, in presence of 50 mM ammonium acetate and 30 mM MgCl2


organism: Prochlorothrix hollandica


organism: Pyrococcus furiosus

substrate_name: ptRNATyr

proof_lines: enzyme subunit RNase P RNA + RNase P protein 21 + RNase P protein 29

proof_lines: from Escherichia coli, enzyme substrate Rnase P RNA

proof_lines: from Escherichia coli, emzyme subunit RNase P RNA + Pop5 + RNase P protein 30

substrate: ptRNATyr


organism: Pyrococcus horikoshii

proof_lines: wild-type enzyme, pH not specified in the publication, 65°C


organism: Saccharolobus solfataricus

substrate_name: tRNA

substrate: tRNA


organism: Saccharomyces cerevisiae

substrate_name: H2O; tRNA precursor

assay_conditions_summary: pH 8; 293.15 K; buffer 10 mM HEPES

proof_lines: pre-tRNA-Tyr with the 3-UUUUU trailer, at 20°C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl

proof_lines: pre-tRNA-Tyr without the 3-UUUUU trailer, at 20°C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl

substrate: H2O; tRNA precursor


organism: Schizosaccharomyces pombe

proof_lines: derived from the sup S1 and sup3-e tRNASer genes of Schizosaccharomyces pombe


organism: Spinacia oleracea

substrate_name: tRNAPhe (G+1) precursor

proof_lines: 37°C, substrate substituted with phosphothionate from GMPaS

substrate: tRNAPhe (G+1) precursor


organism: Thermotoga maritima

substrate_name: tRNATyr precursor

substrate: tRNATyr precursor


organism: Bos taurus

substrate_name: Unknown

proof_lines: inhibition of lysoPLD activity, > 60 microM, size of acyl chain is crucial for the maximal inhibitory action, spectrophotometric assay

proof_lines: > 60 microM, inhibition of lysoPLD activity, spectrophotometric assay

substrate: Unknown


organism: Renibacterium sp. QD1

substrate_name: chitosan

substrate: chitosan


organism: Streptomyces hygroscopicus


organism: Streptomyces sp.

substrate_name: chitohexaose

substrate: chitohexaose


organism: Sus scrofa

proof_lines:
40°C, pH 4, isoform PSC-II
40°C, pH 4, isoform PSC-I
40°C, pH 4, isoform PSC-III


organism: uncultured bacterium


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


organism: Aliivibrio salmonicida

substrate_name: dUMP DNA

substrate: dUMP DNA


organism: Archaeoglobus fulgidus

substrate_name: uracil-mismatched double-stranded DNA

substrate: uracil-mismatched double-stranded DNA


substrate_name: uracil-containing single-stranded DNA

substrate: uracil-containing single-stranded DNA


substrate_name: uracil-containing double-stranded DNA

substrate: uracil-containing double-stranded DNA


organism: Escherichia coli


organism: Gadus morhua

substrate_name: uracil-containing calf thymus DNA

proof_lines:
wild type enzyme, at pH 7.5 and 15°C
wild type enzyme, at pH 7.5 and 22°C
wild type enzyme, at pH 7.5 and 37°C

substrate: uracil-containing calf thymus DNA


organism: Solanum lycopersicum


organism: Solanum tuberosum

substrate_name: diphosphate

substrate: diphosphate


substrate_name: D-Fructose 6-phosphate; Diphosphate

substrate: D-Fructose 6-phosphate; Diphosphate


substrate_name: Diphosphate; D-Fructose 6-phosphate

substrate: Diphosphate; D-Fructose 6-phosphate


organism: Toxoplasma gondii

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Treponema pallidum


organism: Triticum aestivum

proof_lines: versus diphosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration

proof_lines: versus fructose 6-phosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration


organism: Vigna radiata

substrate_name: sedoheptulose 7-phosphate

proof_lines:
pH 8.0, 25°C
forward reaction, pH 8.0, 25°C

substrate: sedoheptulose 7-phosphate


organism: Aspergillus nidulans

substrate_name: pre-tRNAAsp

substrate: pre-tRNAAsp


organism: Bacillus subtilis

substrate_name: tRNA precursor; H2O

proof_lines:
enzyme RNA moiety, pH 7.0
catalyzed by RNase P RNA
catalyzed by circular RNnase P RNA

substrate: tRNA precursor; H2O


organism: Dictyostelium discoideum

substrate_name: pre-tRNA supS1 tRNASer

proof_lines: at 37°C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol

substrate: pre-tRNA supS1 tRNASer


substrate_name: H2O; tRNA precursor

proof_lines:
pH 7.6, 37°C
37°C, pH 8.0
absence of spiramycin

substrate: H2O; tRNA precursor


organism: Carpodesmia tamariscifolia

substrate_name: 4-nitrocatechol sulfate

substrate: 4-nitrocatechol sulfate


organism: Chlamydomonas reinhardtii

substrate_name: 4-nitrophenyl sulfate

proof_lines:
without imidazole
with imidazole

substrate: 4-nitrophenyl sulfate


organism: Citrobacter braakii


organism: Eimeria tenella


organism: Gallus gallus

proof_lines: enzyme from fraction II and fraction III


organism: Haliotis iris

substrate_name: 2-hydroxy-5-nitrophenyl sulfate

proof_lines: in presence of 100 mM acetate and 100 mM sulfate

substrate: 2-hydroxy-5-nitrophenyl sulfate


organism: Helix pomatia

substrate_name: ferulic acid 4-sulfate

proof_lines: pH 7.0, temperature not specified in the publication

substrate: ferulic acid 4-sulfate


organism: Hemicentrotus pulcherrimus


organism: Homo sapiens

proof_lines: pH 5.0, 37°C, patient with cerebral palsy


organism: Littorina kurila

substrate_name: p-Nitrophenyl sulfate

substrate: p-Nitrophenyl sulfate


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


organism: Acinetobacter lwoffii

substrate_name: succinyl-CoA

substrate: succinyl-CoA


organism: Acrididae

substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


organism: Columba sp.

substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


organism: Fasciola hepatica

substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


organism: Lucilia sericata

substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


organism: Oncorhynchus mykiss

substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


organism: Sus scrofa


organism: Rhodospirillum rubrum

substrate_name: phosphate

substrate: phosphate


organism: Ricinus communis

substrate_name: D-fructose 6-phosphate

proof_lines:
forward reaction, pH 7.5, 25°C
reverse reaction, pH 7.8, 25°C
pH 7.8, 25°C

substrate: D-fructose 6-phosphate


organism: Saccharum hybrid cultivar


organism: Sansevieria trifasciata

substrate_name: D-Fructose 6-phosphate; Diphosphate

proof_lines: pH 7.3, reverse reaction, in presence of 2 mM Mg2+

substrate: D-Fructose 6-phosphate; Diphosphate


organism: Hemiscorpius lepturus


substrate_name: lysophosphatidylcholine

proof_lines: kinetic analysis of recombinant autotaxin/lysoPLD using [14C] lysophosphatidylcholine substrate

proof_lines: in presence of 0.25 mM Zn2+ plus 10 mM L-histidine

substrate: lysophosphatidylcholine


proof_lines: substrate p-nitrophenyl thymidine 5-monophosphate, pH 8.0, 30 min of incubation at 37°C, measuring absorbance at 405 nm, twofold higher KI compared to inhibitor S1P


substrate_name: lysophosphatidylcholine 18:0

proof_lines: wild type enzyme, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C

substrate: lysophosphatidylcholine 18:0


substrate_name: lysophosphatidylcholine 16:0

proof_lines: mutant enzyme H420Q, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C

substrate: lysophosphatidylcholine 16:0


proof_lines: mutant enzyme H226Q, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C


proof_lines: mutant enzyme H434Q, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C


organism: Mammalia

substrate_name: coumarin-phosphate-fluorescein

proof_lines: coumarin-phosphate-fluorescein is a fluorescence resonance energy transfer (FRET)-based sensor of phosphodiesterase activity. Very useful substrate for enzymatic analysis of purified autotaxin/lysoPLD and can also be used to detect autotaxi

substrate: coumarin-phosphate-fluorescein


proof_lines: achieved under optimal assay conditions, almost same results in blood plasma

proof_lines: CPF4 FRET assay (change of fluorescence intensity), inihibition involves both a reduction in vmax and an increase in km, binding affinity is 1000fold stronger than to 1-alkyl-sn-glycero-3-phosphoethanolamine and analogue substrates


organism: Rattus norvegicus

proof_lines:
Vmax is 0.019 micromol/min/mg
Vmax is 0.035 micromol/min/mg
Vmax is 0.059 micromol/min/mg


organism: Streptomyces chromofuscus


organism: Aspergillus oryzae


enzyme_display_name: thioredoxin-dependent peroxiredoxin

organism: Treponema pallidum

substrate_name: thioredoxin; cumene hydroperoxide; H2O2; t-butyl hydroperoxide

proof_lines: pH 7.0, 25°C, TpAhpC with cumene hydroperoxide

enzyme: thioredoxin-dependent peroxiredoxin


smiles: OO


substrate_name: t-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: t-butyl hydroperoxide


organism: Trichoderma reesei

proof_lines:
pH 8, 25°C
at pH 7.2 and 30°C


organism: Vibrio vulnificus

substrate_name: reduced thioredoxin A; H2O2

substrate: reduced thioredoxin A; H2O2


organism: Xylella fastidiosa


substrate_name: cumene hydroperoxide; H2O2; t-butyl hydroperoxide


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


organism: Saccharomyces cerevisiae

substrate_name: DELTA1-Pyrroline-5-carboxylate; L-azetidine-2-carboxylic acid; cis-4-hydroxy-L-proline; L-azetidine-2-carboxylate

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

proof_lines:
at pH 7.5 and 30°C
at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y168A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y75A to reconstruct the assayed variant sequence.


substrate_name: L-azetidine-2-carboxylic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y166F to reconstruct the assayed variant sequence.

substrate: L-azetidine-2-carboxylic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y75A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y166F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y157A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature Y89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature R145E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature Y157A to reconstruct the assayed variant sequence.


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature F65G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; buffer 50 mM Tris-HCl; cofactor CoA

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row F65G; column Km (uM) = 140; column kcat (s^-1) = 17; column kcat/Km (s^-1 uM^-1) = 0.12. captured primary segment: Acetyl-CoA | F65G variant Mpr1 | Km 140 uM | kcat 17 s^-1 | kcat/Km 0.12 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 140 uM; 1 uM is 1/1000 mM, giving 0.14 mM; the exported value is 0.14 mM. kcat: printed cell 17 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 17.0 s^(-1); the exported value is 17.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 0.12 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 120.0 s^(-1)*mM^(-1). The exported kcat_over_km 121.42857142857142 s^(-1)*mM^(-1) is the exact full-precision quotient of the two printed cells of this same row, and the printed efficiency cell is that quotient written to the precision the column uses. The quotient of this row's own printed component cells is 17 / 0.14 = 121.42857142857143 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row F65G: Km = 140 uM; kcat = 17 s^-1; printed kcat/Km = 0.12 s^-1 uM^-1.

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63R/L117V to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row KL (K63R/L117V); column Km (mM) = 1.7; column kcat (s^-1) = 46; column kcat/Km (s^-1 mM^-1) = 27. captured primary segment: AZC | KL variant Mpr1 (K63R/L117V) | Km 1.7 mM | kcat 46 s^-1 | kcat/Km 27 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 1.7 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 1.7 mM; the exported value is 1.7 mM. kcat: printed cell 46 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 46.0 s^(-1); the exported value is 46.0 s^(-1). kcat/Km: printed AZC efficiency cell 27 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 27.0 s^(-1)*mM^(-1). The exported kcat_over_km 27.058823529411764 s^(-1)*mM^(-1) is the exact full-precision quotient of the two printed cells of this same row, and the printed efficiency cell is that quotient written to the precision the column uses. The quotient of this row's own printed component cells is 46 / 1.7 = 27.058823529411764 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row KL: Km = 1.7 mM; kcat = 46 s^-1; printed kcat/Km = 27 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63P to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row K63P; column Km (uM) = 19; column kcat (s^-1) = 15; column kcat/Km (s^-1 uM^-1) = 0.80. captured primary segment: Acetyl-CoA | K63P variant Mpr1 | Km 19 uM | kcat 15 s^-1 | kcat/Km 0.80 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 19 uM; 1 uM is 1/1000 mM, giving 0.019 mM; the exported value is 0.019 mM. kcat: printed cell 15 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 15.0 s^(-1); the exported value is 15.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 0.80 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 800.0 s^(-1)*mM^(-1). The exported kcat_over_km is 789.4736842105264 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 15 / 0.019 = 789.4736842105264 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row K63P: Km = 19 uM; kcat = 15 s^-1; printed kcat/Km = 0.80 s^-1 uM^-1.