organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

sequence_source: source_record identity cache for UniProtKB:Q8DNZ8


enzyme_display_name: glutaminase

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

substrate_name: L-glutamine

source_db: uniprot

verification_status: unverified

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_source: source_record identity cache for UniProtKB:Q9X0C8

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

data_origin: experimental

enzyme: glutaminase

substrate: L-glutamine

status: unverified

source: uniprot


organism: Acinetobacter glutaminasificans

substrate_name: L-Gln

source_db: brenda

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

substrate: L-Gln

source: brenda


organism: Aspergillus flavus


organism: Aspergillus fumigatus

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


organism: Aspergillus oryzae


organism: Aspergillus sojae

km_display: Not reported


organism: Bacillus cereus


organism: Arabidopsis thaliana

verification_status: corrected

status: corrected


organism: Bacillus subtilis (strain 168)

substrate_name: ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 2.49 sec(-1) for FGAM synthase activity (at pH 7.2 and 37 degrees Celsius). kcat is 0.002 sec(-1) for glutaminase activity (at pH 7.2 and 37 degrees Celsius).


proof_lines: kcat is 7.60 min(-1) for glutaminase activity.


organism: Plasmodium falciparum (isolate 3D7)


organism: Sporosarcina pasteurii

substrate_name: L-Asn

assay_conditions_summary: pH 9

proof_lines:
pH 9.0, at 37ºC, H2O as co-substrate
pH 9.0, at 37ºC, NH2OH as co-substrate

substrate: L-Asn


organism: Streptomyces roseolus

substrate_name: L-Glutamic acid

substrate: L-Glutamic acid


organism: Streptomyces sp.

substrate_name: L-glutamate

substrate: L-glutamate


organism: Trichoderma reesei

proof_lines: polyacrylic acid-Cu2+-immobilized enzyme, at pH 8.0 and 50°C


organism: Bacillus sp. (in: firmicutes)


organism: Camelus dromedarius


organism: Escherichia coli

substrate_name: gamma-glutamyl methylamide

substrate: gamma-glutamyl methylamide


organism: Geobacillus sp. H6a


organism: Lacticaseibacillus rhamnosus

substrate_name: glutamine

assay_conditions_summary: pH 7

substrate: glutamine


organism: Limosilactobacillus reuteri


organism: Pseudomonas aeruginosa


organism: Pseudomonas chlororaphis subsp. aurantiaca


organism: Rattus norvegicus

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

mutation_type: deletion

assay_conditions_summary: pH 8; buffer acetate/phosphate

proof_lines: recombinant enzyme with N-terminal deletion, T-acetate buffer, pH 8.0

proof_lines: recombinant enzyme with N-terminal deletion, T-phosphate buffer, pH 8.0


assay_conditions_summary: pH 8; buffer phosphate/acetate

proof_lines: recombinant enzyme with N-terminal and C-terminal deletions, T-phosphate buffer, pH 8.0

proof_lines: recombinant enzyme with N-terminal and C-terminal deletions, T-acetate buffer, pH 8.0


substrate_name: Gln

assay_conditions_summary: pH 8

proof_lines:
in presence of 150 mM phosphate
native enzyme, T-acetate buffer, pH 8.0
in presence of 10 mM phosphate

substrate: Gln


organism: Rhizobium etli

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Micrococcus luteus

proof_lines: pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl

proof_lines: pH 7.5, 30°C, full-length enzyme, in absence of NaCl

proof_lines: pH 7.5, 30°C, protease-cleaved large enzyme fragment, in absence of NaCl


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence, reconstructed with selected source mutation Y191T. and applied mutation signature Y191T to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_source: UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence, reconstructed with selected source mutation E160D. and applied mutation signature E160D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4U1A6 canonical Micrococcus luteus K-3 glutaminase sequence, reconstructed with selected source mutation Y191F. and applied mutation signature Y191F to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: succinamate

proof_lines: pH and temperature not specified in the publication

substrate: succinamate


substrate_name: L-Glutamine

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

sequence_source: UniProtKB P17169 canonical sequence checked 2026-06-03; A602L variant requires manual processed-chain coordinate arbitration.

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

assay_conditions_summary: Glutaminase activity measured as Gln hydrolysis in absence of Fru-6P.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant A602L

substrate: L-Glutamine


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature W74L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant W74L


kcat_over_km_origin: calculated

sequence_source: UniProtKB P17169 REST/FASTA checked 2026-06-03.


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature W74F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant W74F


source_db: oed

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature W74A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant W74A


sequence_source: UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants.


sequence_variant_note: Resolved canonical sequence from UniProtKB P17169 REST/FASTA checked 2026-06-03; processed-chain mutation offset +1 used for variants. and applied mutation signature V605L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutaminase(Enzyme) mutant V605L


enzyme_display_name: aspartate carbamoyltransferase

organism: Homo sapiens

substrate_name: dihydroorotate

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

enzyme: aspartate carbamoyltransferase

substrate: dihydroorotate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

assay_conditions_summary: cofactor ATP


organism: Bacillus subtilis

substrate_name: Carbamoyl phosphate; L-Aspartate

sequence_source: UniProtKB:P05654 FASTA retrieved 2026-06-03

substrate: Carbamoyl phosphate; L-Aspartate


organism: Enterococcus faecalis

substrate_name: L-Aspartate; Carbamoyl phosphate

sequence_source: UniProtKB:Q9L4T8 FASTA retrieved 2026-06-03

substrate: L-Aspartate; Carbamoyl phosphate


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

sequence_source: UniProtKB:P0A786 FASTA retrieved 2026-06-03

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=8.3


organism: Mesocricetus auratus

proof_lines: SABIO-RK modifier species: aspartate carbamoyltransferase(Enzyme) mutant D90A N-terminal His6-tag


proof_lines: SABIO-RK modifier species: aspartate carbamoyltransferase(Enzyme) mutant R269A N-terminal His6-tag


substrate_name: L-Aspartate

sequence_source: UniProtKB:P08955 FASTA retrieved 2026-06-03

substrate: L-Aspartate


substrate_name: Carbamoyl phosphate

smiles: NC(=O)OP(=O)(O)O

substrate: Carbamoyl phosphate


enzyme_display_name: histidine decarboxylase

organism: Clostridium perfringens

substrate_name: L-Histidine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature K172I with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant K172I

enzyme: histidine decarboxylase

substrate: L-Histidine


sequence_source: UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature S96T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S96T


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature Y280F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant Y280F


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature I74E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant I74E


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature F98A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant F98A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature E81Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E81Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0TU55, reviewed Swiss-Prot DCHS_CLOP1, Clostridium perfringens histidine decarboxylase proenzyme, EC 4.1.1.22 and applied mutation signature Y77F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant Y77F


organism: Lactobacillus sp.

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature E197D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E197D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature E66Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E66Q


sequence_source: UniProtKB:P00862 REST direct check on 2026-06-03

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 UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature E197Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E197Q


sequence_variant_note: Mutation signature S82C matches the mutant residue at offset +1 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S82C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00862 REST direct check on 2026-06-03 and applied mutation signature S82T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S82T


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P00862 sequence with reviewer-computed S82T substitution and applied mutation signature S82T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P00862 sequence with reviewer-computed S82C substitution and applied mutation signature S82C to reconstruct the assayed variant sequence.


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

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant G58D


sequence_source: UniProt REST accession P00862 reviewed canonical sequence fetched during worker7 review

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=4.8


organism: Morganella morganii

sequence_source: UniProt REST accession P05034 reviewed canonical sequence fetched during worker7 review


sequence_source: UniProt REST accession P23738 reviewed canonical sequence fetched during worker7 review


organism: Oenococcus oeni

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


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

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E214H


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S97T


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E214D


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant D78A


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant E214I


substrate_name: L-Histidine; L-Dopa

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant C-terminal truncated (2-477)

substrate: L-Histidine; L-Dopa


sequence_variant_note: Mutation signature S354G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant C180S/C418S C-terminal truncated (2-477)


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-Dopa

substrate: L-Dopa


proof_lines: SABIO-RK modifier species: histidine decarboxylase(Enzyme) mutant S354G C-terminal truncated (2-477)


source_db: skid

mutation_signature: truncation

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.8
Raw SKiD Env: Temp=-----, pH=-----

source: skid


organism: Lactobacillus buchneri


organism: Lactobacillus sp. (strain 30a)


substrate_name: histidine

substrate: histidine


sequence_source: UniProtKB:P16453 canonical displayed sequence


enzyme_display_name: carboxymethylproline synthase

organism: Pectobacterium carotovorum subsp. carotovorum

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 sec(-1) with malonyl-CoA as substrate. kcat is 1.52 sec(-1) with (S)-1-pyrroline-5-carboxylate as substrate.

enzyme: carboxymethylproline synthase

substrate: malonyl-CoA


organism: Pectobacterium carotovorum

sequence_source: UniProtKB reviewed accession Q9XB60 from direct EC/name/organism lookup on 2026-06-03

assay_conditions_summary: pH 7.8; 295.15 K; buffer a piperazine/HEPES; cofactor CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'malonyl-CoA' whose reaction cell reads (2S,5S)-CMPr formation; column 'kcat (s-1)' = 1.7 ± 0.2; column 'Km (mM)' = 0.0027 ± 0.0009; column 'kcat/Km (mM-1 s-1)' = 630.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.0027 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.0027 mM; the exported value is 0.0015 mM, which Table 1 prints in its L-P5C body row. kcat: printed Table 1 cell 1.7 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.7 s^(-1); the exported value is 1.7 s^(-1). kcat/Km: printed Table 1 cell 630 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 630.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 1.7 / 0.0027 = 629.6296296296297 s^-1 mM^-1, and the article's own printed efficiency cell is 630 s^-1 mM^-1, which this record carries.

raw_value_unit_evidence: Table 1, body row 'malonyl-CoA', reaction '(2S,5S)-CMPr formation': kcat = 1.7 ± 0.2 s^-1; Km = 0.0027 ± 0.0009 mM; printed kcat/Km = 630 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'malonyl-CoA' and reaction '(2S,5S)-CMPr formation'

table_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0 (Biochemistry 2004, volume 43, issue 50, pages 15936-15945)


enzyme_display_name: Carboxymethylproline synthase

organism: Erwinia carotovora

substrate_name: Malonyl-CoA

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA

enzyme: Carboxymethylproline synthase

substrate: Malonyl-CoA


assay_conditions_summary: pH 8; 295.15 K; buffer a piperazine/HEPES; cofactor CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'L-pyrroline-5-carboxylate'; column 'reaction' = (2S,5S)-CMPr formation; column 'kcat (s-1)' = 1.52 ± 0.04; column 'Km (mM)' = 0.0015 ± 0.0004; column 'kcat/Km (mM-1 s-1)' = 984.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.0015 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.0015 mM; the exported value is 0.002 mM. kcat: printed Table 1 cell 1.52 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.52 s^(-1); the exported value is 1.52 s^(-1). kcat/Km: printed Table 1 cell 984 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 984.0 s^(-1)*mM^(-1); the exported value is 760.0 s^(-1)*mM^(-1), the quotient of the exported kcat and the exported Km. Closure disclosure: the quotient of the two printed component cells is 1.52 / 0.0015 = 1013.3333333333334 s^-1 mM^-1, and the article's own printed efficiency cell is 984 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'L-pyrroline-5-carboxylate', reaction '(2S,5S)-CMPr formation': kcat = 1.52 ± 0.04 s^-1; Km = 0.0015 ± 0.0004 mM; printed kcat/Km = 984 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'L-pyrroline-5-carboxylate' and reaction '(2S,5S)-CMPr formation'


substrate_name: Propanoyl-CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'propionyl-CoA'; column 'reaction' = hydrolysis; column 'kcat (s-1)' = 0.190 ± 0.009; column 'Km (mM)' = 1.7 ± 0.2; column 'kcat/Km (mM-1 s-1)' = 0.110.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.7 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.7 mM; the exported value is 1.7 mM. kcat: printed Table 1 cell 0.190 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.19 s^(-1); the exported value is 0.19 s^(-1). kcat/Km: printed Table 1 cell 0.110 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.11 s^(-1)*mM^(-1); the exported value is 0.11176470588235295 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.19 / 1.7 = 0.11176470588235295 s^-1 mM^-1, and the article's own printed efficiency cell is 0.110 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'propionyl-CoA', reaction 'hydrolysis': kcat = 0.190 ± 0.009 s^-1; Km = 1.7 ± 0.2 mM; printed kcat/Km = 0.110 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'propionyl-CoA' and reaction 'hydrolysis'

substrate: Propanoyl-CoA


substrate_name: Acetyl-CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'acetyl-CoA'; column 'reaction' = hydrolysis; column 'kcat (s-1)' = 0.043 ± 0.002; column 'Km (mM)' = 5.4 ± 0.7; column 'kcat/Km (mM-1 s-1)' = 0.0081.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.4 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 5.4 mM; the exported value is 5.4 mM. kcat: printed Table 1 cell 0.043 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.043 s^(-1); the exported value is 0.043 s^(-1). kcat/Km: printed Table 1 cell 0.0081 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.0081 s^(-1)*mM^(-1); the exported value is 0.007962962962962962 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.043 / 5.4 = 0.007962962962962962 s^-1 mM^-1, and the article's own printed efficiency cell is 0.0081 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'acetyl-CoA', reaction 'hydrolysis': kcat = 0.043 ± 0.002 s^-1; Km = 5.4 ± 0.7 mM; printed kcat/Km = 0.0081 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'acetyl-CoA' and reaction 'hydrolysis'

substrate: Acetyl-CoA


column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'methylmalonyl-CoA' carrying footnote marker c; column 'reaction' = decarboxylation; column 'kcat (s-1)' = 0.07 ± 0.01; column 'Km (mM)' = 0.6 ± 0.3; column 'kcat/Km (mM-1 s-1)' = 0.10.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.6 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.6 mM; the exported value is 0.6 mM. kcat: printed Table 1 cell 0.07 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.07 s^(-1); the exported value is 0.07 s^(-1). kcat/Km: printed Table 1 cell 0.10 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.1 s^(-1)*mM^(-1); the exported value is 0.11666666666666668 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.07 / 0.6 = 0.11666666666666668 s^-1 mM^-1, and the article's own printed efficiency cell is 0.10 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'methylmalonyl-CoA', reaction 'decarboxylation': kcat = 0.07 ± 0.01 s^-1; Km = 0.6 ± 0.3 mM; printed kcat/Km = 0.10 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'methylmalonyl-CoA' and reaction 'decarboxylation'


substrate_name: Carboxymethylproline-CoA

column_label: Table 1: Steady-State Kinetic Parameters for CarB Measured at 22 °C and pH 8.0, body row 'CMPr-CoA'; column 'reaction' = hydrolysis; column 'kcat (s-1)' = 0.53 ± 0.05; column 'Km (mM)' = 0.009 ± 0.002; column 'kcat/Km (mM-1 s-1)' = 58.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.009 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.009 mM; the exported value is 0.009 mM. kcat: printed Table 1 cell 0.53 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.53 s^(-1); the exported value is 0.53 s^(-1). kcat/Km: printed Table 1 cell 58 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 58.0 s^(-1)*mM^(-1); the exported value is 58.88888888888889 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells. Closure disclosure: that quotient is 0.53 / 0.009 = 58.88888888888889 s^-1 mM^-1, and the article's own printed efficiency cell is 58 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 1, body row 'CMPr-CoA', reaction 'hydrolysis': kcat = 0.53 ± 0.05 s^-1; Km = 0.009 ± 0.002 mM; printed kcat/Km = 58 mM^-1 s^-1.

row_label: Table 1, body row with substrate 'CMPr-CoA' and reaction 'hydrolysis'

substrate: Carboxymethylproline-CoA


enzyme_display_name: steroid 21-monooxygenase

sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature P31Q to reconstruct the assayed variant sequence.

proof_lines: mutant P31Q, pH not specified in the publication, temperature not specified in the publication

enzyme: steroid 21-monooxygenase


substrate_name: progesterone

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature G65E to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'G65E', clinical phenotype column 'SW', substrate column 'progesterone'; column 'kcat' with unit head 'min^-1' = 3.6; column 'Km' with unit head 'uM' = 5.5; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 0.67; column 'Catalytic efficiency' with unit head '% wild type' = 0.082.

normalized_value_unit_evidence: kcat: printed cell 3.6 min^-1; 3.6 / 60 = 0.060000000000000005 s^-1; this pass carries 0.06 s^(-1) and the exported value is 0.062 s^(-1). Km: printed cell 5.5 uM; 5.5 / 1000 = 0.0055 mM; the exported value is 0.0055 mM. kcat/Km: printed cell 0.67 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.67 * 1000 / 60 = 11.166666666666668 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row G65E with substrate progesterone: printed kcat cell 3.6 in the column headed kcat, printed unit min^-1; printed Km cell 5.5 in the column headed Km, printed unit uM; printed kcat/Km cell 0.67 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row G65E with substrate progesterone

table_label: Table 2: Catalytic activities of 21A2 variants (J. Biol. Chem. 2017, 292(26):10767-10778)

substrate: progesterone


sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature V282L to reconstruct the assayed variant sequence.

proof_lines: mutant V282L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature I172N to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'I172N', clinical phenotype column 'SV', substrate column '17alpha-OH-progesterone'; column 'kcat' with unit head 'min^-1' = 0.18; column 'Km' with unit head 'uM' = 4.9; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 0.037; column 'Catalytic efficiency' with unit head '% wild type' = 0.023.

normalized_value_unit_evidence: kcat: printed cell 0.18 min^-1; 0.18 / 60 = 0.003 s^-1; the exported value is 0.003 s^(-1). Km: printed cell 4.9 uM; 4.9 / 1000 = 0.004900000000000001 mM; this pass carries 0.0049 mM and the exported value is 0.0018 mM. kcat/Km: printed cell 0.037 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.037 * 1000 / 60 = 0.6166666666666667 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row I172N with substrate 17alpha-OH-progesterone: printed kcat cell 0.18 in the column headed kcat, printed unit min^-1; printed Km cell 4.9 in the column headed Km, printed unit uM; printed kcat/Km cell 0.037 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row I172N with substrate 17alpha-OH-progesterone


sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature G292C to reconstruct the assayed variant sequence.

proof_lines: mutant G292C, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature L108R to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'L108R', clinical phenotype column 'SW', substrate column 'progesterone'; column 'kcat' with unit head 'min^-1' = 0.0059; column 'Km' with unit head 'uM' = 2.7; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 0.0022; column 'Catalytic efficiency' with unit head '% wild type' = 0.00027.

normalized_value_unit_evidence: kcat: printed cell 0.0059 min^-1; 0.0059 / 60 = 0.00009833333333333333 s^-1; the exported value is 0.0001 s^(-1), which is that quotient at the precision the export carries. Km: printed cell 2.7 uM; 2.7 / 1000 = 0.0027 mM; this pass carries 0.0027 mM and the exported value is 0.0017 mM. kcat/Km: printed cell 0.0022 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.0022 * 1000 / 60 = 0.036666666666666674 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row L108R with substrate progesterone: printed kcat cell 0.0059 in the column headed kcat, printed unit min^-1; printed Km cell 2.7 in the column headed Km, printed unit uM; printed kcat/Km cell 0.0022 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row L108R with substrate progesterone


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08686 and applied mutation signature P31L to reconstruct the assayed variant sequence.

column_label: Table 2 (Catalytic activities of 21A2 variants), variant row 'P31L', clinical phenotype column 'NC', substrate column '17alpha-OH-progesterone'; column 'kcat' with unit head 'min^-1' = 84; column 'Km' with unit head 'uM' = 1.7; column 'kcat/Km' with unit head 'uM^-1 min^-1' = 49; column 'Catalytic efficiency' with unit head '% wild type' = 30.

normalized_value_unit_evidence: kcat: printed cell 84 min^-1; 84 / 60 = 1.4 s^-1; the exported value is 1.4 s^(-1). Km: printed cell 1.7 uM; 1.7 / 1000 = 0.0017 mM; this pass carries 0.0017 mM and the exported value is 0.0012 mM. kcat/Km: printed cell 49 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 49 * 1000 / 60 = 816.6666666666667 s^-1 mM^-1; the catalog row carries no catalytic-efficiency value, so this printed cell is kept as typed primary_reported provenance and no ratio is exported.

raw_value_unit_evidence: Table 2 (Catalytic activities of 21A2 variants), variant row P31L with substrate 17alpha-OH-progesterone: printed kcat cell 84 in the column headed kcat, printed unit min^-1; printed Km cell 1.7 in the column headed Km, printed unit uM; printed kcat/Km cell 49 in the column headed kcat/Km, printed unit uM^-1 min^-1.

row_label: Table 2, variant row P31L with substrate 17alpha-OH-progesterone


sequence_variant_note: Resolved canonical sequence from UniProt P08686 canonical sequence fetched directly; variant reconstructed from selected BRENDA mutation note and validated canonical residue. and applied mutation signature R357W to reconstruct the assayed variant sequence.

proof_lines: mutant R357W, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: mevalonate kinase

substrate_name: Mevalonate; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature T243A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant T243A

enzyme: mevalonate kinase

substrate: Mevalonate; ATP


substrate_name: ATP; Mevalonate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature S146A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant S146A

substrate: ATP; Mevalonate


substrate_name: (R)-mevalonate

sequence_source: UniProtKB Q03426 canonical FASTA retrieved directly for identity context; row-specific variant sequence not reconstructed

substrate: (R)-mevalonate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature I56A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature I196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature Y149A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03426 canonical FASTA retrieved directly; variant reconstructed locally from the selected mutation signature and applied mutation signature T104A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; not accepted as row sequence because the selected source context mixes two variants.


sequence_source: UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03.

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


substrate_name: ATP; (R)-Mevalonate

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: UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; preserved as identity context only because the selected row does not expose a wild-type or mutation-specific state.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

source_databases_merged: sabio_rk brenda skid

substrate: ATP; (R)-Mevalonate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation D204A. and applied mutation signature D204A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant D204A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation E296Q. and applied mutation signature E296Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant E296Q


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation E193Q. and applied mutation signature E193Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant E193Q


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation E19D. and applied mutation signature E19D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant E19D


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q03426 checked directly via UniProt REST on 2026-06-03; variant reconstructed from SABIO-RK source mutation D204N. and applied mutation signature D204N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant D204N


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature A334T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant A334T chimeric protein with Glutathione S-transferase


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature N301T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant N301T chimeric protein with Glutathione S-transferase


organism: Methanocaldococcus jannaschii


organism: Rattus norvegicus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines:
liver mevalonate kinase
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K13M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant K13M


organism: Staphylococcus aureus


enzyme_display_name: sphingosine kinase

organism: Arabidopsis thaliana

substrate_name: Sphingosine kinase 1; Dioleoyl phosphatidic acid

enzyme: sphingosine kinase


organism: Homo sapiens

substrate_name: ATP; Sphingosine

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines:
isoform SphK1, at pH 7.4 and 23Â°C
as bovine serum albumin complex
pH 7.4, 30°C, recombinant isozyme SPHK2

substrate: ATP; Sphingosine


organism: Bos taurus

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P00191, checked 2026-06-03 and applied mutation signature T241R/L442A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession P00191, checked 2026-06-03

proof_lines: pH 7.4, 37°C, CYP21 wild-type and mutant T241R/L442A


substrate_name: H+; Progesterone; NADPH; O2

sequence_source: UniProtKB REST accession P00191, checked 2026-06-03; canonical sequence retained as context only

proof_lines: SABIO-RK modifier species: steroid 21-monooxygenase(Enzyme) mutant C3B21RA N-terminal His6-tag

substrate: H+; Progesterone; NADPH; O2


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

proof_lines: 37°C, pH 7.4, presence of 0.002% Cymal 5

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P08686, checked 2026-06-03 and applied mutation signature V470A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P08686, checked 2026-06-03 and applied mutation signature V359A to reconstruct the assayed variant sequence.


substrate_name: sphingosine

sequence_source: UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03.

substrate: sphingosine


substrate_name: D-erythro-sphingosine

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature S79A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant S79A

substrate: D-erythro-sphingosine


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature G113A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant G113A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature E180Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant E180Q


sequence_source: Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note.

sequence_variant_note: Mutation signature Δ364 references residue 364, which is outside the resolved sequence length.

proof_lines: pH and temperature not specified in the publication, deletion mutant DELTA364-384


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature E182Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant E182Q


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature K27A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant K27A


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q9NYA1/SPHK1_HUMAN canonical FASTA, fetched 2026-06-03, using the selected BRENDA mutation note. and applied mutation signature K29A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant K29A

substrate: ATP


sequence_source: UniProtKB:P08686 direct REST lookup on 2026-06-03

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

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08686 direct REST lookup plus R409C reconstruction on 2026-06-03 and applied mutation signature R409C to reconstruct the assayed variant sequence.

proof_lines: mutant R409C, pH not specified in the publication, temperature not specified in the publication


organism: Bacopa monnieri

sequence_source: UniProtKB:M1F2U2 direct REST lookup on 2026-06-03


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


organism: Enterococcus faecalis

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03426 direct REST lookup plus S201A reconstruction on 2026-06-03 and applied mutation signature S201A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant S201A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03426 direct REST lookup plus S145A reconstruction on 2026-06-03 and applied mutation signature S145A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mevalonate kinase(Enzyme) mutant S145A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K103R to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant K103R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D178N to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant D178N


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G26A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant G26A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D176N to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant D176N


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G82A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant G82A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D81N to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D81N enzyme, pH and temperature not specified in the publication


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


assay_conditions_summary: pH 7.4; 355.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature V470A/I471A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature V359G to reconstruct the assayed variant sequence.


sequence_source: Direct UniProt REST/FASTA lookup on 2026-06-03: reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence for Homo sapiens CYP21A2, EC 1.14.14.16.


substrate_name: NADPH; H+; O2; Progesterone

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines:
recombinant enzyme, at pH 7.4 and 37°C
pH 7.4, 35°C
pH 7.4, 37°C

substrate: NADPH; H+; O2; Progesterone


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature T296N to reconstruct the assayed variant sequence.

proof_lines: mutant T296N, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature W303R to reconstruct the assayed variant sequence.

proof_lines: mutant W303R, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from reviewed UniProtKB P08686/CP21A_HUMAN canonical sequence fetched on 2026-06-03 and the selected row mutation signature. and applied mutation signature G292S to reconstruct the assayed variant sequence.

proof_lines: mutant G292S, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession Q9NRA0 direct lookup on 2026-06-03

proof_lines: in 50 mM HEPES, pH 7.4, 10 mM KCl, 15 mM MgCl2, 0.1% Triton X-100, 20% glycerol, 2 mM orthovanadate, 2 mM dithiothreitol, 10 mM NaF, and 1 mM deoxypyridoxine

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


organism: Mus musculus

substrate_name: Sphingosine; ATP

sequence_source: UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03

substrate: Sphingosine; ATP


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

sequence_source: UniProtKB reviewed accession Q9JIA7 direct lookup on 2026-06-03

proof_lines: about, pH 7.4, 30°C, recombinant isozyme SPHK1a


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature D175N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme and mutant E181Q


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature E181Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature D177N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature E179Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: Unknown

sequence_source: UniProtKB:Q1HGK5 direct REST lookup; PMID 18028875 cross-check

substrate: Unknown


sequence_source: UniProtKB:Q91V26 direct REST lookup; PMID 9575218 PubMed cross-check


organism: Saccharomyces cerevisiae

substrate_name: Sphinganine; ATP

sequence_source: UniProtKB:Q12246 direct REST lookup; PMID 9677363 PubMed/UniProt cross-check

substrate: Sphinganine; ATP


sequence_source: UniProtKB:Q06147 direct REST lookup; PMID 9677363 PubMed/UniProt cross-check


enzyme_display_name: (d)CMP kinase

organism: Escherichia coli

substrate_name: dCMP

sequence_variant_note: Resolved canonical sequence from RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; variant reconstructed from checked P0A6I0 sequence and applied mutation signature R181M to reconstruct the assayed variant sequence.

enzyme: (d)CMP kinase

substrate: dCMP


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; variant reconstructed from checked P0A6I0 sequence and applied mutation signature S101A to reconstruct the assayed variant sequence.


sequence_source: RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; canonical sequence from P0A6I0


substrate_name: CMP

sequence_variant_note: Resolved canonical sequence from RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; variant reconstructed from checked P0A6I0 sequence and applied mutation signature D185A to reconstruct the assayed variant sequence.

substrate: CMP


substrate_name: UMP

sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132S substitution and applied mutation signature D132S to reconstruct the assayed variant sequence.

substrate: UMP


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132A substitution and applied mutation signature D132A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132A substitution


substrate_name: ATP; CMP

sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132H substitution and applied mutation signature D132H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132H

substrate: ATP; CMP


sequence_source: UniProt REST accession P0A6I0 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied R110M substitution and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132N substitution and applied mutation signature D132N to reconstruct the assayed variant sequence.


sequence_source: UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132S substitution


organism: Escherichia coli K-12

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature R110M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row R110M, nucleotide dCMP: column Km (mM) = 7.3; column kcat (s^-1) = 0.05; column kcat/Km (s^-1 mM^-1) = 0.0068.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.05 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.05 s^(-1). Km: printed Table 2 cell 7.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 7.3 mM. kcat/Km: printed Table 2 cell 0.0068 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 0.0068 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row R110M, nucleotide dCMP: Km = 7.3 mM; kcat = 0.05 s^-1; printed kcat/Km = 0.0068 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature D132H to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row D132H, nucleotide dCMP: column Km (mM) = 0.055; column kcat (s^-1) = 0.06; column kcat/Km (s^-1 mM^-1) = 1.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.06 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.06 s^(-1). Km: printed Table 2 cell 0.055 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.055 mM. kcat/Km: printed Table 2 cell 1.1 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 1.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row D132H, nucleotide dCMP: Km = 0.055 mM; kcat = 0.06 s^-1; printed kcat/Km = 1.1 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature D132N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature R188M to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row R188M, nucleotide dCMP: column Km (mM) = 0.77; column kcat (s^-1) = 0.04; column kcat/Km (s^-1 mM^-1) = 0.052.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.04 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.04 s^(-1). Km: printed Table 2 cell 0.77 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.77 mM. kcat/Km: printed Table 2 cell 0.052 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 0.052 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row R188M, nucleotide dCMP: Km = 0.77 mM; kcat = 0.04 s^-1; printed kcat/Km = 0.052 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature D132S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature D132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature S36A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant S36A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D132N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature R188M to reconstruct the assayed variant sequence.


substrate_name: CMP; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature R110M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant R110M

substrate: CMP; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature D132A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature D132A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row D132A, nucleotide dCMP: column Km (mM) = 1.8; column kcat (s^-1) = 0.73; column kcat/Km (s^-1 mM^-1) = 0.40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.73 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.73 s^(-1). Km: printed Table 2 cell 1.8 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.8 mM. kcat/Km: printed Table 2 cell 0.40 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 0.40 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row D132A, nucleotide dCMP: Km = 1.8 mM; kcat = 0.73 s^-1; printed kcat/Km = 0.40 s^-1 mM^-1.


sequence_source: UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03

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 UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature R188M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature D132S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature D132N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132N


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature R188M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature R188M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03

proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature D132A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature S36A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


enzyme_display_name: Cytidylate kinase / CMP kinase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132N reconstructed by direct residue substitution. and applied mutation signature D132N to reconstruct the assayed variant sequence.

enzyme: Cytidylate kinase / CMP kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132H reconstructed by direct residue substitution. and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; R110M reconstructed by direct residue substitution. and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132S reconstructed by direct residue substitution. and applied mutation signature D132S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_source: UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; R110M reconstructed by direct residue substitution.


sequence_source: UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132N reconstructed by direct residue substitution.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature D132A to reconstruct the assayed variant sequence.

row_label: Table 2, enzyme row D132A, nucleotide dCMP

table_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373)


source_db: brenda, skid

sequence_source: UniProtKB:P0A6I0 canonical sequence checked 2026-06-03.

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

proof_lines: in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C

source: brenda, skid


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WPA9

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


enzyme_display_name: estrone sulfotransferase

organism: Cavia porcellus

substrate_name: Estrone; 3'-Phosphoadenylyl sulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature S262A/D264A/N267A and applied mutation signature S262A/D264A/N267A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant S262A D264A N267A

enzyme: estrone sulfotransferase

substrate: Estrone; 3'-Phosphoadenylyl sulfate


sequence_source: UniProtKB reviewed accession P49887


substrate_name: 3'-Phosphoadenylyl sulfate; Estrone

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G263A and applied mutation signature G263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G263A

substrate: 3'-Phosphoadenylyl sulfate; Estrone


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature S262A/D264A and applied mutation signature S262A/D264A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant S262A D264A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G260A/K266A and applied mutation signature G260A/K266A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G260A K266A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G260A and applied mutation signature G260A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G260A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G263A/K266A and applied mutation signature G263A/K266A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G263A K266A


sequence_source: UniProtKB:P0A6I0 REST lookup

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature D132H and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature S36A and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature R188M and applied mutation signature R188M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant R188M


sequence_source: reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature D132H


proof_lines:
wild-type enzyme
wild type


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature D132S and applied mutation signature D132S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature T51V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant T51V


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K106R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K106R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K106A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K106A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K48R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K48R


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

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant H108K GST-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K106S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K106S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature Y240F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant Y240F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature T52V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant T52V


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49887/ST1E1_CAVPO; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature K266A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K266A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49887/ST1E1_CAVPO; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature G260A/G263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G260A G263A


sequence_source: UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03

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

assay_conditions_summary: pH 6.5; 310.15 K; buffer 50 mM Tris/HCl

proof_lines: SULT1E1, pH and temperature not specified in the publication

proof_lines: isoform SULT1E1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature V145E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant V145E His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature K85A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K85A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature S137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant hEST S137A


substrate_name: 3'-Phosphoadenylyl sulfate

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

substrate: 3'-Phosphoadenylyl sulfate


substrate_name: nitrobenzoxadiazole-labeled sphingosine

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

proof_lines: pH 7.4, 35°C, presence of 25 microM 3-O-sulfogalactosylceramide

proof_lines: pH 7.4, 35°C, presence of 10 microM 3-O-sulfogalactosylceramide

substrate: nitrobenzoxadiazole-labeled sphingosine


organism: Unknown

substrate_name: estradiol

substrate: estradiol


substrate_name: progesterone

substrate: progesterone


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

substrate_name: (RS)-mevalonate (at 70 degrees Celsius)

smiles: CC(CCO)(CC(=O)[O-])O

substrate: (RS)-mevalonate (at 70 degrees Celsius)


substrate_name: (R,S)-mevalonate

substrate: (R,S)-mevalonate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: mevalonate

substrate: mevalonate


substrate_name: sphingosine

proof_lines: kcat is 124 sec(-1) for sphingosine and increases to 304 sec(-1) upon interaction with EEF1A1.

substrate: sphingosine


substrate_name: Acetyl-CoA (in presence of 10 uM of sphingosine)

proof_lines: kcat is 0.0185 min(-1) for Acetyl-CoA as substrate.


proof_lines: kcat is 55 min(-1) with (24S)-hydroxycholesterol.


substrate_name: PAPS

proof_lines: kcat is 23.5 sec(-1) with estradiol as substrate.

substrate: PAPS


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


assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific S137C reconstruction and applied mutation signature S137C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific S137C reconstruction

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant hEST S137C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K reconstruction and applied mutation signature E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_source: UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup

proof_lines: wild type enzyme, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific K85E/A135T/F138Y/G182S/L251V reconstruction and applied mutation signature K85E/A135T/F138Y/G182S/L251V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K85E/A135T/F138Y/G182S/L251V, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific D65N/K85E/E86K/F138Y reconstruction and applied mutation signature D65N/K85E/E86K/F138Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D65N/K85E/E86K/F138Y, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_source: UniProtKB reviewed P49891 / ST1E1_MOUSE direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49891 / ST1E1_MOUSE direct REST lookup with row-specific T45V reconstruction and applied mutation signature T45V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant T45V


substrate_name: phytosphingosine

substrate: phytosphingosine


substrate_name: dihydrosphingosine

substrate: dihydrosphingosine


substrate_name: sphinganine

substrate: sphinganine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: CMP

substrate: CMP


proof_lines: mutant enzyme D322G, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


proof_lines: mutant enzyme A265V, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


organism: Oncorhynchus mykiss

proof_lines:
liver microsomes
head kidney microsomes


organism: Aedes aegypti

substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

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

substrate: ATP


organism: Agave americana


organism: Homo sapiens

proof_lines: pH 7.5, 30°C, recombinant S201A mevalonate kinase


proof_lines: pH 7.5, 30°C, recombinant S145A mutant mevalonate kinase

proof_lines: pH 7.5, 30°C, recombinant S145A mevalonate kinase


proof_lines: pH 7.5, 30°C, recombinant T243A mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific E19D reconstruction and applied mutation signature E19D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific D204N reconstruction and applied mutation signature D204N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific E296Q reconstruction and applied mutation signature E296Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific E193Q reconstruction and applied mutation signature E193Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup

proof_lines: pH 7.0, 25°C, recombinant mevalonate kinase


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q58487 / MVK_METJA direct REST lookup with row-specific K272R reconstruction and applied mutation signature K272R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 307.15 K; cofactor ATP

proof_lines: pH 7.5, 34°C, K272R mutant mevalonate kinase


sequence_source: UniProtKB Q58487 direct lookup resolved the Methanocaldococcus jannaschii mevalonate kinase canonical sequence; no row-specific R196L variant sequence was accepted because the paper names Arg196Lys instead.

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

proof_lines: pH 7.5, 34°C, R196L mutant mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue R196 to V after confirming residue 196=R. and applied mutation signature R196V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 34°C, R196V mutant mevalonate kinase


sequence_source: UniProtKB Q58487 direct lookup resolved the canonical wild-type mevalonate kinase sequence.

proof_lines: pH 8.0, 70°C, recombinant mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue R196 to Q after confirming residue 196=R. and applied mutation signature R196Q to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 34°C, R196Q mutant mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue K272 to A after confirming residue 272=K. and applied mutation signature K272A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 34°C, K272A mutant mevalonate kinase


substrate_name: (R)-mevalonate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue C281 to A after confirming residue 281=C. and applied mutation signature C281A to reconstruct the assayed variant sequence.

substrate: (R)-mevalonate


organism: Methanosarcina mazei

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

assay_conditions_summary: pH 7.6; 303.15 K; cofactor ATP

proof_lines: apparent value, in 50 mM Tris, 50 mM NaCl (pH 7.6), at 30°C


organism: Oryctolagus cuniculus

substrate_name: DL-mevalonate

substrate: DL-mevalonate


organism: Phaseolus vulgaris

proof_lines: pH 7.0, 30°C, enzyme from etiolated cotyledons


organism: Pinus pinaster

assay_conditions_summary: pH 7.9; 310.15 K; cofactor ATP


organism: Rattus norvegicus

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines:
H20Y mutant enzyme enzyme, pH 7.5, 25°C
H20Y mutant enzyme, pH 7.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107A/C281A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03

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 UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C281S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107S/C281S to reconstruct the assayed variant sequence.


organism: Arachis hypogaea

substrate_name: (R)-Mevalonate; ATP

assay_conditions_summary: cofactor ATP

substrate: (R)-Mevalonate; ATP


organism: Catharanthus roseus


organism: Cucumis melo


organism: Enterococcus faecalis

substrate_name: GTP

sequence_source: NCBI Protein NP_814642.1; PMID 14767074 / PMC2286734 paper names NP_814642 as the E. faecalis mvaK1 open reading frame and reports the expressed mevalonate kinase.

assay_conditions_summary: pH 10; 310.15 K; cofactor ATP

substrate: GTP


organism: Hevea brasiliensis


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03426 canonical human MVK sequence; reconstructed S146A using PMID 11278915 and the selected BRENDA note. and applied mutation signature S146A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant S146A mevalonate kinase


organism: Sarcophaga bullata


organism: Staphylococcus aureus

substrate_name: R,S-mevalonate

proof_lines: PMID 14679225 full text reports R,S-mevalonate Km 41 ± 3 μM under pH 7.5, 30°C assay context.

substrate: R,S-mevalonate


organism: Sus scrofa

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0
liver mevalonate kinase
pH 6.5, 30°C, at 1 mM Mg2+


substrate_name: D-(+)-erythro-sphinganine

substrate: D-(+)-erythro-sphinganine


organism: Tetrahymena pyriformis


organism: Bacillus subtilis

proof_lines: at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH


organism: Escherichia coli

substrate_name: dGMP

proof_lines:
reaction with ATP
pH 7.4, 30°C
pH 7.4, reaction with CMP

substrate: dGMP


organism: Mycobacterium tuberculosis

substrate_name: dCMP

proof_lines: pH and temperature not specified in the publication

substrate: dCMP


organism: Bos taurus


organism: Cavia porcellus

proof_lines:
pH 7.4, 37°C
pH 7.4, 37°C, competitive inhibition


organism: Homo sapiens

substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from direct_uniprot_lookup:P49888_with_K85A_reconstruction and applied mutation signature K85A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 37°C, SULT1E1-K85A
pH 7.0, 37°C, mutant SULT1E1-K85A

substrate: dehydroepiandrosterone


proof_lines:
pH 7.0, 25°C
ATP in form of MgATP2-
native enzyme, pH 7.5, 25°C


proof_lines: pH 7.0, 30°C, K13M mutant mevalonate kinase


organism: Ricinus communis


organism: Saccharomyces cerevisiae


substrate_name: estrone

sequence_variant_note: Resolved canonical sequence from UniProtKB:P49888 reviewed human SULT1E1 canonical sequence; PubMed 11006110 describes human SULT1E1 V145E mutagenesis; direct residue check found P49888 residue 145 is V. and applied mutation signature V145E to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 37°C, SULT1E1-V145E
pH 7.0, 37°C, mutant SULT1E1-V145E

substrate: estrone


sequence_source: UniProtKB:P49888 reviewed human SULT1E1 canonical sequence from direct EC 2.8.2.4 + Homo sapiens lookup.

proof_lines:
pH 6.1, 25°C
pH 6.3, 37°C forward reaction
pH 6.3, 37°C, reverse reaction


organism: Mus musculus

substrate_name: estradiol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence; selected BRENDA note and PubMed 10514486 identify Y81L estrogen sulfotransferase mutagenesis; direct residue check found P49891 residue 81 is Y. and applied mutation signature Y81L to reconstruct the assayed variant sequence.

substrate: estradiol


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence; selected BRENDA note and PubMed 10514486 identify Y81L/F142L estrogen sulfotransferase mutagenesis; direct residue check found P49891 residues 81=Y and 142=F. and applied mutation signature Y81L/F142L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence; selected BRENDA note and PubMed 10514486 identify Y81F estrogen sulfotransferase mutagenesis; direct residue check found P49891 residue 81 is Y. and applied mutation signature Y81F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence from direct EC 2.8.2.4 + Mus musculus lookup.


substrate_name: androstenediol

sequence_variant_note: Resolved canonical sequence from Reconstructed F142L from UniProtKB reviewed P49891 (ST1E1_MOUSE) after direct residue check; RCSB 1AQU maps murine estrogen sulfotransferase to P49891 with full UniProt coverage. and applied mutation signature F142L to reconstruct the assayed variant sequence.

substrate: androstenediol


sequence_variant_note: Resolved canonical sequence from Reconstructed Y81A from UniProtKB reviewed P49891 (ST1E1_MOUSE); PubMed 10514486 studies Tyr-81 EST mutants and RCSB 1AQU maps murine estrogen sulfotransferase to P49891. and applied mutation signature Y81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed F142A from UniProtKB reviewed P49891 (ST1E1_MOUSE); PubMed 10514486 studies Phe-142 EST mutants and RCSB 1AQU maps murine estrogen sulfotransferase to P49891. and applied mutation signature F142A to reconstruct the assayed variant sequence.


organism: Rattus norvegicus


substrate_name: gamma-undecanoiclactone

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

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM Tris

proof_lines: isozyme 192Q, in 50 mM HEPES (pH 7.4), 37°C

substrate: gamma-undecanoiclactone


organism: Clonostachys rosea

substrate_name: zearalenone

sequence_variant_note: Resolved canonical sequence from Reconstructed V153H from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature V153H to reconstruct the assayed variant sequence.

substrate: zearalenone


sequence_variant_note: Resolved canonical sequence from Reconstructed F222K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature F222K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D157K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D157K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed V158H from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature V158H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D133K/D157K/E171K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D133K/D157K/E171K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D133K/D157K/E171K, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed D133K/D157K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D133K/D157K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D133K/D157K, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed N152K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature N152K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D57K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D57K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature E145K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature E171K to reconstruct the assayed variant sequence.