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


enzyme_display_name: acylglycerol lipase

organism: Homo sapiens

source_db: oed

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

enzyme: acylglycerol lipase

source: oed


mutation_signature: Unknown

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


organism: Caenorhabditis elegans

substrate_name: Unknown

source_db: uniprot

kcat_display: Not reported

km_display: Not reported

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

substrate: Unknown

source: uniprot


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

data_origin: experimental


substrate_name: 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in absence of BSA)


substrate_name: p-nitrophenyl acetate

verification_status: unverified

substrate: p-nitrophenyl acetate

status: unverified


source_db: brenda

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q99685 plus direct H54A reconstruction and applied mutation signature H54A to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q99685 plus direct H49A reconstruction and applied mutation signature H49A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q99685 plus direct H272Y reconstruction and applied mutation signature H272Y to reconstruct the assayed variant sequence.


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q99685 plus direct H272A reconstruction and applied mutation signature H272A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed entry Q99685 plus direct H49A reconstruction


organism: Mus musculus

substrate_name: sn-1-Monooleoylglycerol; H2O

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

sequence_source: UniProtKB reviewed entry O35678

substrate: sn-1-Monooleoylglycerol; H2O


substrate_name: H2O; sn-1-Monooleoylglycerol

sequence_source: UniProtKB reviewed entry Q8R2Y0

substrate: H2O; sn-1-Monooleoylglycerol


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed entry Q8R431

assay_conditions_summary: 310.15 K; buffer TME


proof_lines: kcat is 21 min(-1) with 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol).


organism: Arabidopsis thaliana

substrate_name: monoacylglycerol

proof_lines:
pH 8.0, 30°C, AtMAGL15
pH 8.0, 30°C, AtMAGL14
pH 8.0, 30°C, AtMAGL10

substrate: monoacylglycerol


organism: Bacillus sp. (in: firmicutes)


substrate_name: 4-nitrophenyl acetate

proof_lines: pH and temperature not specified in the publication

proof_lines: at pH 8 and 25°C, in 10% dimethyl sulfoxide

substrate: 4-nitrophenyl acetate


substrate_name: retinyl palmitate

substrate: retinyl palmitate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: palmitoyl-MAG

substrate: palmitoyl-MAG


substrate_name: 4-Methylumbelliferyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProt Q99685 FASTA plus selected row mutation signature and applied mutation signature L169S/L176S/K226A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169S/L176S/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C

substrate: 4-Methylumbelliferyl butyrate


sequence_variant_note: Resolved canonical sequence from UniProt Q99685 FASTA plus selected row mutation signature and applied mutation signature L167Q/L174Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L167Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt Q99685 FASTA plus selected row mutation signature and applied mutation signature L171Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt Q99685 FASTA plus selected row mutation signature and applied mutation signature L169S/L176S/K165A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169S/L176S/K165A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_source: UniProt Q99685 FASTA direct check

proof_lines: wild type enzyme, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt Q99685 FASTA plus selected row mutation signature and applied mutation signature L169S/L176S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169S/L176S, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q99685 and applied mutation signature L171Q to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic Constants (Protein Science 2011, volume 20, pages 670-683); printed column heads Construct | KM (uM) | kcat (min^-1) | kcat/KM (uM^-1 min^-1), 4-Methylumbelliferyl butyrate block. Table II, 4-Methylumbelliferyl butyrate block, construct row 1-303 Leu171Gln; column KM (uM) = 105; column kcat (min^-1) = 51; column kcat/KM (uM^-1 min^-1) = 0.48. captured primary segment: 1-303 Leu171Gln | KM 105 uM | kcat 51 min^-1 | kcat/KM 0.48 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table II KM cell 105 uM; 1 uM is 1/1000 mM, so 105 / 1000 = 0.105 mM. kcat: printed Table II kcat cell 51 min^-1; 1 min^-1 is 1/60 s^-1, so 51 / 60 = 0.85 s^(-1). kcat/Km: printed Table II kcat/KM cell 0.48 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 mM^-1 divided by 60 s, that is 16.666666666666668 s^-1 mM^-1, so 0.48 x 1000 / 60 = 8.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.85 / 0.105 = 8.095238095238095 s^-1 mM^-1, against the printed catalytic-efficiency cell 8.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, 4-Methylumbelliferyl butyrate block, construct row 1-303 Leu171Gln: KM = 105 uM; kcat = 51 min^-1; printed kcat/KM = 0.48 uM^-1 min^-1.

status: corrected


substrate_name: prostaglandin E2-G

proof_lines: in the presence of 0.0003 mM pristimerin, at pH 7.5, 37°C

substrate: prostaglandin E2-G


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q8R431|PMID:19486005|C242G and applied mutation signature C242G to reconstruct the assayed variant sequence.


enzyme_display_name: plasmin

organism: Unknown

substrate_name: tosyl-Arg methyl ester

enzyme: plasmin

substrate: tosyl-Arg methyl ester


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with mutation_signature applied during review and applied mutation signature L169S/L176S/K160A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169S/L176S/K160A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_source: UniProtKB Q99685 canonical sequence with mutation_signature applied during review


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with mutation_signature applied during review and applied mutation signature L169S/L176S/K36A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169S/L176S/K36A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q99685 and applied mutation signature L171Q/L174Q to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic Constants (Protein Science 2011, volume 20, pages 670-683); printed column heads Construct | KM (uM) | kcat (min^-1) | kcat/KM (uM^-1 min^-1), 4-Methylumbelliferyl butyrate block. Table II, 4-Methylumbelliferyl butyrate block, construct row 1-303 Leu171Gln, Leu174Gln; column KM (uM) = 89; column kcat (min^-1) = 47; column kcat/KM (uM^-1 min^-1) = 0.52. captured primary segment: 1-303 Leu171Gln, Leu174Gln | KM 89 uM | kcat 47 min^-1 | kcat/KM 0.52 uM^-1 min^-1

raw_value_unit_evidence: Table II, 4-Methylumbelliferyl butyrate block, construct row 1-303 Leu171Gln, Leu174Gln: KM = 89 uM; kcat = 47 min^-1; printed kcat/KM = 0.52 uM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with mutation_signature applied during review and applied mutation signature L171Q/L174Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L171Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with mutation_signature applied during review and applied mutation signature L167Q/L174Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with mutation_signature applied during review and applied mutation signature L167Q/L171Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L167Q/L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q99685 and applied mutation signature L169S/L176S/K36A/K226A to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic Constants (Protein Science 2011, volume 20, pages 670-683); printed column heads Construct | KM (uM) | kcat (min^-1) | kcat/KM (uM^-1 min^-1), 4-Methylumbelliferyl butyrate block. Table II, 4-Methylumbelliferyl butyrate block, construct row 1-303 Leu169Ser, Leu176Ser, Lys36Ala, Lys226Ala; column KM (uM) = 123; column kcat (min^-1) = 30; column kcat/KM (uM^-1 min^-1) = 0.25. captured primary segment: 1-303 Leu169Ser, Leu176Ser, Lys36Ala, Lys226Ala | KM 123 uM | kcat 30 min^-1 | kcat/KM 0.25 uM^-1 min^-1

raw_value_unit_evidence: Table II, 4-Methylumbelliferyl butyrate block, construct row 1-303 Leu169Ser, Leu176Ser, Lys36Ala, Lys226Ala: KM = 123 uM; kcat = 30 min^-1; printed kcat/KM = 0.25 uM^-1 min^-1.


organism: Bos taurus

ki_unit: mM

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


substrate_name: D-Val-Leu-Lys-p-nitroanilide; H2O

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

sequence_source: UniProtKB reviewed entry P00747 (PLMN_HUMAN), direct accession lookup

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

substrate: D-Val-Leu-Lys-p-nitroanilide; H2O


organism: Sus scrofa

substrate_name: N-Ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester; H2O

sequence_source: UniProtKB reviewed entry P06867 (PLMN_PIG), direct accession lookup


proof_lines:
pH 8.0
Val561-plasminogen
native enzyme


mutation_signature: deletion mutant lacking the middle portion of the protein

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

mutation_type: deletion


mutation_signature: truncated delta-plasmin

mutation_type: truncation

proof_lines: truncated delta-plasmin, in phosphate buffered saline, pH 7.4, at 25°C


organism: Oryctolagus cuniculus

proof_lines:
plasmin 1
plasmin 2
plasmin 1 and plasmin 2


organism: synthetic construct

proof_lines:
in the presence of 0.065 mM stearate
in the absence of fatty acids
in the presence of 0.01 mM oleate


organism: Bacillus sp. (strain H-257)

sequence_source: Direct UniProtKB reviewed accession P82597 lookup.

proof_lines: in 10 mM Tris-HCl (pH 7.2), temperature not specified in the publication


substrate_name: 2-Arachidonoylglycerol; H2O / mixed source substrates

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

sequence_source: Direct UniProtKB reviewed accession Q99685 lookup.

assay_conditions_summary: pH 7.4; 310.15 K; buffer TME

proof_lines: recombinant enzyme, in TME buffer, at 37°C

source_databases_merged: sabio_rk brenda skid


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with row-specific mutation reconstruction from PMID 21308848 construct labels. and applied mutation signature L169S/L176S/K36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with row-specific mutation reconstruction from PMID 21308848 construct labels. and applied mutation signature L169S/L176S/K226A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with row-specific mutation reconstruction from PMID 21308848 construct labels. and applied mutation signature L167Q/L171Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with row-specific mutation reconstruction from PMID 21308848 construct labels. and applied mutation signature L169S/L176S/K36A/K226A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169S/L176S/K36A/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with row-specific mutation reconstruction from PMID 21308848 construct labels. and applied mutation signature L169S/L176S/K165A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99685 canonical sequence with row-specific mutation reconstruction from PMID 21308848 construct labels. and applied mutation signature L169S/L176S to reconstruct the assayed variant sequence.


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

substrate_name: succinate semialdehyde (SSA)

proof_lines: kcat is 61.5 sec(-1) for NAD as substrate.

substrate: succinate semialdehyde (SSA)


organism: Azospirillum brasilense

substrate_name: alpha-ketoglutaric semialdehyde (in the presence of NAD(+), at 25 degrees Celsius and pH 7.2)

proof_lines: The catalytic efficiency with alphaKGSA in the presence of NAD(+) is 5.2- and 6.2-fold higher than with succinic semialdehyde and glutaraldehyde, respectively. When NADP(+) is used as a cosubstrate, the catalytic efficiency with alphaKGSA d


organism: Acinetobacter baylyi

substrate_name: NAD+; Succinate semialdehyde; H2O

sequence_source: UniProt REST direct accession lookup Q6F9G0

substrate: NAD+; Succinate semialdehyde; H2O


substrate_name: NAD(+) (at 24 degrees Celsius)

verification_status: verified

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

assay_conditions_summary: pH 9; 297.15 K; cofactor NAD+

substrate: NAD(+) (at 24 degrees Celsius)

status: verified


organism: Saccharolobus solfataricus

substrate_name: succinate semialdehyde

sequence_source: UniProtKB REST/FASTA direct lookup for Q97XS9

smiles: O=CCCC(=O)O

substrate: succinate semialdehyde


substrate_name: NAD+

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+

substrate: NAD+


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


enzyme_display_name: complement subcomponent C1s

organism: Homo sapiens

substrate_name: complement component C2

proof_lines: kcat is 7.4 sec(-1) for component C2. Less efficient than MASP2 in C4 cleavage.

enzyme: complement subcomponent C1s

substrate: complement component C2


substrate_name: complement component C2 P4-P1 fragment

sequence_source: UniProtKB reviewed accession P09871 (C1S_HUMAN), queried by EC 3.4.21.42 and organism_id:9606 during review.

proof_lines: 145 mM NaCl, 50 mM triethanolamine hydrochloride, 1 mM CaCl2, 1 mg/ml OVA pH 7.4, 37°C

proof_lines: 145 mM NaCl, 50 mM triethanolamine hydrochloride, 1 mM CaCl2, 1 mg/ml ovalbumin pH 7.4, 37°C

substrate: complement component C2 P4-P1 fragment


substrate_name: Unknown

substrate: Unknown


substrate_name: N-Acetyl-Gly-Lys methyl ester

sequence_source: UniProtKB reviewed accession P09871 (C1S_HUMAN), checked 2026-06-08

substrate: N-Acetyl-Gly-Lys methyl ester


substrate_name: Complement component C4; H2O

substrate: Complement component C4; H2O


substrate_name: Complement component C2; H2O

substrate: Complement component C2; H2O


substrate_name: N-Benzoyl-L-arginine ethyl ester; H2O

proof_lines: pH and temperature not specified in the publication

substrate: N-Benzoyl-L-arginine ethyl ester; H2O


substrate_name: p-Tosyl-L-arginine methyl ester

substrate: p-Tosyl-L-arginine methyl ester


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 7.4, 37°C, recombinant wild-type enzyme


organism: Lumbricus rubellus

substrate_name: acetaldehyde

assay_conditions_summary: cofactor NAD+

substrate: acetaldehyde


organism: Mus musculus


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

proof_lines: mutant enzyme R166H, at 37°C, in 40 mM sodium phosphate, pH 7.4


proof_lines: mutant enzyme R166E, at 37°C, in 40 mM sodium phosphate, pH 7.4


proof_lines: mutant enzyme R166A, at 37°C, in 40 mM sodium phosphate, pH 7.4


proof_lines: mutant enzyme R166K, at 37°C, in 40 mM sodium phosphate, pH 7.4


proof_lines: wild type enzyme, at 37°C, in 40 mM sodium phosphate, pH 7.4


organism: Rhipicephalus microplus

substrate_name: n-Pentanal

assay_conditions_summary: pH 8.5; 295.15 K; buffer 100 mM Na2HPO4/NaH2PO4

proof_lines: in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C

substrate: n-Pentanal


organism: Solanum tuberosum


organism: Triticum turgidum subsp. durum


organism: Aspergillus niger

assay_conditions_summary: pH 9; 310.15 K; cofactor NAD+

proof_lines:
pH 9.0 37°C
pH 9.0, 37°C
pH 9.0, 37°C, versus NAD+


substrate_name: Glutaraldehyde

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADP+

proof_lines: 1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C

proof_lines: 1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25°C

substrate: Glutaraldehyde


organism: Drosophila melanogaster

assay_conditions_summary: cofactor NADP+


substrate_name: NAD+; H2O; Succinate semialdehyde

substrate: NAD+; H2O; Succinate semialdehyde


organism: Lucilia cuprina


assay_conditions_summary: pH 8.5; 295.15 K; buffer 100 mM Na2HPO4/NaH2PO4; cofactor NAD+


substrate_name: NAD+; H2O; Succinate semialdehyde methyl ester


organism: Escherichia coli K-12

assay_conditions_summary: pH 9; 310.15 K; cofactor NADP+


organism: Euglena gracilis

assay_conditions_summary: pH 8.3; 308.15 K; cofactor NAD+


substrate_name: propionaldehyde

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+

proof_lines: 50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25°C

proof_lines: succinate semialdehyde as varied substrate

substrate: propionaldehyde


organism: Hordeum vulgare subsp. vulgare


enzyme_display_name: 3'(2'),5'-bisphosphate nucleotidase

organism: Chromobacterium violaceum

substrate_name: 2'-deoxycytidine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pCp`: kcat (s^-1) = 9.4; Km (uM) = 26; kcat/Km (M^-1 s^-1) = 3.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.4 s^-1 is already the export unit, so no conversion is needed; the exported value is 9.4 s^(-1). Km: printed Table 3 cell 26 uM; 26 / 1000 = 0.026 mM; the exported value is 0.026 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 3.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.6 x 10^5 / 1000 = 360.0 s^(-1)*mM^(-1); the exported value is 361.53846153846155 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pCp`

enzyme: 3'(2'),5'-bisphosphate nucleotidase

substrate: 2'-deoxycytidine 3',5'-bisphosphate


substrate_name: guanosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pGp (footnote a)`: kcat (s^-1) = 12.3; Km (uM) = 17.3; kcat/Km (M^-1 s^-1) = 7.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.3 s^-1 is already the export unit, so no conversion is needed; the exported value is 12.3 s^(-1). Km: printed Table 3 cell 17.3 uM; 17.3 / 1000 = 0.0173 mM; the exported value is 0.0173 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 7.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.1 x 10^5 / 1000 = 710.0 s^(-1)*mM^(-1); the exported value is 710.9826589595376 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pGp (footnote a)`

substrate: guanosine 3',5'-bisphosphate


substrate_name: 2'-Deoxyguanosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pGp`: kcat (s^-1) = 4.2; Km (uM) = 5.2; kcat/Km (M^-1 s^-1) = 7.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.2 s^-1 is already the export unit, so no conversion is needed; the exported value is 4.2 s^(-1). Km: printed Table 3 cell 5.2 uM; 5.2 / 1000 = 0.0052 mM; the exported value is 0.0052 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 7.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^5 / 1000 = 790.0 s^(-1)*mM^(-1); the exported value is 807.6923076923077 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pGp`

substrate: 2'-Deoxyguanosine 3',5'-bisphosphate


substrate_name: 2'-deoxyadenosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pAp`: kcat (s^-1) = 7.1; Km (uM) = 10.2; kcat/Km (M^-1 s^-1) = 7.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 7.1 s^-1 is already the export unit, so no conversion is needed; the exported value is 7.1 s^(-1). Km: printed Table 3 cell 10.2 uM; 10.2 / 1000 = 0.0102 mM; the exported value is 0.0102 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 7.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.0 x 10^5 / 1000 = 700.0 s^(-1)*mM^(-1); the exported value is 696.078431372549 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pAp`

substrate: 2'-deoxyadenosine 3',5'-bisphosphate


substrate_name: uridine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pUp (footnote a)`: kcat (s^-1) = 5.4; Km (uM) = 8.8; kcat/Km (M^-1 s^-1) = 6.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.4 s^-1 is already the export unit, so no conversion is needed; the exported value is 5.4 s^(-1). Km: printed Table 3 cell 8.8 uM; 8.8 / 1000 = 0.0088 mM; the exported value is 0.0088 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 6.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.1 x 10^5 / 1000 = 610.0 s^(-1)*mM^(-1); the exported value is 613.6363636363636 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pUp (footnote a)`

substrate: uridine 3',5'-bisphosphate


substrate_name: adenosine 3',5'-bisphosphate

substrate: adenosine 3',5'-bisphosphate


substrate_name: 2'-Deoxyuridine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pUp`: kcat (s^-1) = 5.2; Km (uM) = 29; kcat/Km (M^-1 s^-1) = 1.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.2 s^-1 is already the export unit, so no conversion is needed; the exported value is 5.2 s^(-1). Km: printed Table 3 cell 29 uM; 29 / 1000 = 0.029 mM; the exported value is 0.029 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 1.8 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.8 x 10^5 / 1000 = 180.0 s^(-1)*mM^(-1); the exported value is 179.3103448275862 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pUp`

substrate: 2'-Deoxyuridine 3',5'-bisphosphate


substrate_name: 2'-deoxythymidine 3',5'-bisphosphate

sequence_source: UniProtKB REST direct lookup:Q7NXD4

substrate: 2'-deoxythymidine 3',5'-bisphosphate


substrate_name: thymidine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pTp`: kcat (s^-1) = 3.3; Km (uM) = 9.3; kcat/Km (M^-1 s^-1) = 3.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.3 s^-1 is already the export unit, so no conversion is needed; the exported value is 3.3 s^(-1). Km: printed Table 3 cell 9.3 uM; 9.3 / 1000 = 0.0093 mM; the exported value is 0.0093 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 3.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.6 x 10^5 / 1000 = 360.0 s^(-1)*mM^(-1); the exported value is 354.8387096774194 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pTp`

substrate: thymidine 3',5'-bisphosphate


organism: Escherichia coli

substrate_name: adenosine 2',5'-bisphosphate

sequence_source: UniProtKB REST direct lookup:P22255

substrate: adenosine 2',5'-bisphosphate


substrate_name: Adenosine 3',5'-bisphosphate

substrate: Adenosine 3',5'-bisphosphate


organism: Mycoplasma pneumoniae


organism: Thermus thermophilus

sequence_source: UniProt REST primaryAccession Q5SM25 canonical sequence


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Escherichia coli (strain K12)


organism: Bacillus subtilis (strain 168)

substrate_name: Unknown

proof_lines: The 2',3'-cyclic phosphodiesterase activity is higher than that of the 5'-nucleotidase with the four major nucleotides used as substrates.

substrate: Unknown


substrate_name: Cytidine 3'-phosphate

sequence_source: UniProt REST uniprotkb/P0A840, checked 2026-06-08; matches identity reuse cache accession:P0A840

substrate: Cytidine 3'-phosphate


substrate_name: Adenosine 3'-phosphate

substrate: Adenosine 3'-phosphate


sequence_source: UniProt REST uniprotkb/P08331, checked 2026-06-08


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

substrate_name: ssDNA 3-mers

proof_lines: kcat for ss nucleic acids decreases about 5 orders of magnitude as chain length increases from 3-mers to 21-mers.

substrate: ssDNA 3-mers


organism: Arabidopsis thaliana


substrate_name: PAP

substrate: PAP


organism: Mus musculus

substrate_name: 3'-phosphoadenosine 5'- phosphate (PAP)

substrate: 3'-phosphoadenosine 5'- phosphate (PAP)


organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)

substrate_name: ssDNA 6-mers in the presence of Mg(2+)

substrate: ssDNA 6-mers in the presence of Mg(2+)


organism: Oryza sativa

substrate_name: 3'-phosphoadenylyl sulfate

substrate: 3'-phosphoadenylyl sulfate


substrate_name: H2O; Adenosine 3',5'-bisphosphate

sequence_source: UniProtKB:P75144 direct accession lookup

substrate: H2O; Adenosine 3',5'-bisphosphate


sequence_source: UniProtKB:P0C5A3 direct accession lookup


organism: Pyrococcus yayanosii

sequence_variant_note: Resolved canonical sequence from UniProtKB:F8AEF2 direct accession lookup plus reconstructed R259A variant and applied mutation signature R259A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F8AEF2 direct accession lookup plus reconstructed D12A variant and applied mutation signature D12A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F8AEF2 direct accession lookup plus reconstructed G285D variant and applied mutation signature G285D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F8AEF2 direct accession lookup plus reconstructed K287A variant and applied mutation signature K287A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:F8AEF2 direct accession lookup

proof_lines: pH 8.0, 70°C, recombinant wild-type enzyme


organism: Rattus norvegicus

sequence_source: UniProtKB:Q9Z1N4 direct accession lookup


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

sequence_source: UniProt exact accession Q7NXD4 direct check on 2026-06-08

proof_lines:
pH 7.5, 3°C
Raw SKiD Env: Temp=3°C, pH=7.5

source_databases_merged: brenda skid


sequence_source: UniProt exact accession P22255 direct check and accession reuse cache


organism: Homo sapiens

sequence_source: UniProt exact accession O95861 direct check and accession reuse cache

proof_lines: pH 7.5, 30°C, substrate: adenosine 3’,5’-bisphosphate

proof_lines: pH 7.5, 30°C, substrate: inositol-1,4-bisphosphate


organism: Limnospira platensis

sequence_source: UniProt exact accession Q3LS17 direct check on 2026-06-08

assay_conditions_summary: pH 8; 303.15 K; cofactor ADP

proof_lines: in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30°C


substrate_name: Adenosine 3',5'-bisphosphate; H2O

sequence_source: UniProt exact accession Q9Z0S1 direct check and accession reuse cache

proof_lines:
recombinant enzyme
native enzyme

substrate: Adenosine 3',5'-bisphosphate; H2O


mutation_signature: Δ1

proof_lines: SABIO-RK modifier species: 3'(2'),5'-bisphosphate nucleotidase(Enzyme) mutant delta1-55, C-terminal His6-tag


sequence_source: UniProt exact accession Q80V26 direct check and accession reuse cache

proof_lines: in 50 mM Bis-Tris (pH 6.5), 0.05 mM MnCl2, 100 mM KCl


organism: Mycobacterium tuberculosis

substrate_name: H2O; D-Fructose 1,6-bisphosphate

sequence_source: UniProt exact accession P9WKJ1 direct check and accession reuse cache

assay_conditions_summary: pH 8.5; buffer 50 mM Tris

proof_lines: in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+

substrate: H2O; D-Fructose 1,6-bisphosphate


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB exact accession lookup P32179; source accession shared by SABIO-RK, BRENDA, and SKiD records

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


sequence_source: UniProtKB exact accession lookup Q5SM25; source accession from SABIO-RK record


organism: Zea mays

substrate_name: adenosine 3',5'-bisphosphate

sequence_source: UniProtKB exact accession lookup Q94G04; source accession from BRENDA records

substrate: adenosine 3',5'-bisphosphate


sequence_source: UniProtKB exact accession lookup Q94FY6; source accession from BRENDA records


substrate_name: 1D-myo-inositol 1,4-bisphosphate

proof_lines: KM for adenosine 3',5'-bisphosphate is between 2 and 10 uM.

substrate: 1D-myo-inositol 1,4-bisphosphate


proof_lines: KM for adenosine 3',5'-bisphosphate is below 1 uM.


substrate_name: adenosine 3',5'-bisphosphate (PAP)

proof_lines: The different methodology used for determination of the hydrolysis of inositol-1,4-bisphosphate might account for the discrepancy obtained with protein homologs from human and rat, which show much more efficiency with this substrate.

substrate: adenosine 3',5'-bisphosphate (PAP)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 3'-phosphoadenosine 5'-phosphate (at pH 9.0 and 30 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: The second-order rate constant for PAP was determined to be over 3 orders of magnitude greater than those determined for IMP and FBP.


proof_lines: KM for adenosine 3',5'-bisphosphate is below 2 uM.


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

proof_lines: KM for adenosine 3',5'-bisphosphate is below 10 uM.


substrate_name: inositol 1,4-bisphosphate

substrate: inositol 1,4-bisphosphate


organism: Auxenochlorella pyrenoidosa


organism: Debaryomyces hansenii

proof_lines: wild type enzyme, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30°C


proof_lines: mutant enzyme E301K, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30°C


proof_lines: mutant enzyme V131A, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30°C


organism: Escherichia coli

substrate_name: D-fructose 1,6-bisphosphate

assay_conditions_summary: pH 7; cofactor NADP+

substrate: D-fructose 1,6-bisphosphate


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB reviewed accession O94505; PubMed 10850973; GenBank D86983


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Leishmania amazonensis

proof_lines:
at pH 7.4 and 25°C
pH 7.4, 25°C


organism: Leishmania donovani


organism: Lolium multiflorum


organism: Solanum tuberosum


substrate_name: Adenosine 3'-phosphate; H2O

sequence_source: UniProtKB P0A840 REST lookup on 2026-06-08; reviewed SURE_ECOLI canonical sequence.

substrate: Adenosine 3'-phosphate; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB P08331 REST lookup on 2026-06-08 with Y544A substitution reconstructed from the selected source note. and applied mutation signature Y544A to reconstruct the assayed variant sequence.


proof_lines: pH 7.5, 37°C, mature enzyme CpdB, substrate 3-AMP


sequence_source: UniProtKB P08331 REST lookup on 2026-06-08; reviewed CPDB_ECOLI canonical sequence.

proof_lines: substrate 3-AMP, wild-type, pH 7.5, 37°C


sequence_source: UniProtKB A0A0K0VK53 REST lookup on 2026-06-08 with H117A paper-coordinate mapped to mature-fragment position 98.

sequence_variant_note: Mutation signature H117A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 37°C, mutant H117A N-terminal domain of CpdB


sequence_source: UniProtKB A0A0K0VK53 REST lookup on 2026-06-08 with Y544A paper-coordinate mapped to mature-fragment position 525.

sequence_variant_note: Mutation signature Y544A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 37°C, mutant Y544A N-terminal domain of CpdB


sequence_source: UniProtKB P08331 residues 20-354 reconstructed from direct UniProt sequence using PMC7922932 CpdB_Ndom boundaries.

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

proof_lines: isolated N-terminal domain, pH 7.5, 37°C


sequence_source: UniProtKB F6MDM5 REST lookup on 2026-06-08; unreviewed Leishmania amazonensis canonical sequence.

proof_lines: apparent Km, whole cell assay, absence of CuCl2, pH 7.4, 25°C

proof_lines: apparent Km, whole cell assay, presence of 0.1 mM CuCl2, pH 7.4, 25°C


enzyme_display_name: thioglucosidase

organism: Arabidopsis thaliana

substrate_name: sinigrin

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

proof_lines:
pH 5.5, isozyme TGG1
pH 5.5, isozyme TGG5
pH 5.5, isozyme TGG4

enzyme: thioglucosidase

substrate: sinigrin


organism: Brassica napus

proof_lines:
30°C, pH 6.8
isoenzyme RC, without ascorbic acid
isoenzyme RB, without ascorbic acid


organism: Sinapis alba

proof_lines:
with dioxane as solvent
with acetonitrile as solvent
with 12.5 M methanol as solvent


substrate_name: sinigrin (at pH 4.5)

substrate: sinigrin (at pH 4.5)


organism: Brevicoryne brassicae

substrate_name: allylglucosinolate

substrate: allylglucosinolate


substrate_name: sinigrin (at pH 4.5 and 37 degrees Celsius)


organism: Aspergillus niger

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: Aspergillus sydowii

substrate_name: p-nitrophenyl-beta-D-glucoside

substrate: p-nitrophenyl-beta-D-glucoside


organism: Brassica juncea

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

proof_lines: in presence of 0.05 M NaCl and 1 mM ascorbate


organism: Brassica oleracea

proof_lines: sinigrin substrate inhibition, Michaelis-Menten modelling, pH 7.0, 40°C


organism: Brassica rapa


organism: Raphanus sativus

proof_lines:
in absence of ascorbate
in presence of 0.5 mM ascorbate


substrate_name: Sinigrin

substrate: Sinigrin


proof_lines: recombinant enzyme TGG2, pH 5.5, 37°C, in presence of ascorbate


proof_lines: recombinant enzyme TGG1, pH 5.5, 37°C, in presence of ascorbate


organism: Armoracia rusticana


substrate_name: gluconasturtiin

substrate: gluconasturtiin


organism: Crambe hispanica subsp. abyssinica

proof_lines:
37°C, without ascorbic acid
37°C, with 20 mM ascorbic acid


organism: Enterobacter cloacae


organism: Lepidium latifolium

proof_lines:
pH 6.0, 37°C, with 1 mM GSH
pH 6.0, 37°C, without GSH


organism: Lepidium sativum


organism: Phyllotreta armoraciae

proof_lines:
isoform Myr1, at pH 6.5 and 27°C
isoform Myr3, at pH 6.5 and 27°C
isoform Myr2, at pH 6.5 and 27°C


organism: Rahnella inusitata

proof_lines:
at pH 7.0 and 40°C
unit: ml/mg/s, at pH 7.0 and 40°C


organism: Escherichia coli (strain K12)

substrate_name: isochorismate (at 22.5 degrees Celsius and pH 7.8)


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature L493A to reconstruct the assayed variant sequence.

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

column_label: Table 2: Steady-state kinetic parameters with respect to alpha-ketoglutarate (2-oxoglutarate), Bacillus subtilis MenD; Protein row 'L493A'; column 'Km (uM)' = 18; column 'kcat (min^-1)' = 10; column 'kcat/Km (uM^-1 min^-1)' = 0.5; column 'Relative kcat/Km' = 0.8.

raw_value_unit_evidence: Table 2, Protein row 'L493A': Km = 18 uM; kcat = 10 min^-1; printed kcat/Km = 0.5 uM^-1 min^-1.

row_label: Table 2, row L493A


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P23970 and applied mutation signature R32A to reconstruct the assayed variant sequence.


substrate_name: Isochorismate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature R32A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'R32A'; column 'Km (uM)' = 49; column 'kcat (min^-1)' = 11; column 'kcat/Km (uM^-1 min^-1)' = 0.22; column 'Relative kcat/Km' = 0.01.

raw_value_unit_evidence: Table 3, Protein row 'R32A': Km = 49 uM; kcat = 11 min^-1; printed kcat/Km = 0.22 uM^-1 min^-1.

row_label: Table 3, row R32A

substrate: Isochorismate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature I489A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'I489A'; column 'Km (uM)' = 27; column 'kcat (min^-1)' = 5.7; column 'kcat/Km (uM^-1 min^-1)' = 0.21; column 'Relative kcat/Km' = 0.01.

raw_value_unit_evidence: Table 3, Protein row 'I489A': Km = 27 uM; kcat = 5.7 min^-1; printed kcat/Km = 0.21 uM^-1 min^-1.

row_label: Table 3, row I489A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature R409A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'R409A'; column 'Km (uM)' = 8.5; column 'kcat (min^-1)' = 1.4; column 'kcat/Km (uM^-1 min^-1)' = 0.16; column 'Relative kcat/Km' = 0.009.

raw_value_unit_evidence: Table 3, Protein row 'R409A': Km = 8.5 uM; kcat = 1.4 min^-1; printed kcat/Km = 0.16 uM^-1 min^-1.

row_label: Table 3, row R409A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature F490A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'F490A'; column 'Km (uM)' = 29; column 'kcat (min^-1)' = 1.7; column 'kcat/Km (uM^-1 min^-1)' = 0.058; column 'Relative kcat/Km' = 0.003.

raw_value_unit_evidence: Table 3, Protein row 'F490A': Km = 29 uM; kcat = 1.7 min^-1; printed kcat/Km = 0.058 uM^-1 min^-1.

row_label: Table 3, row F490A


column_label: Table 2: Steady-state kinetic parameters with respect to alpha-ketoglutarate (2-oxoglutarate), Bacillus subtilis MenD; Protein row 'F490A'; column 'Km (uM)' = 274; column 'kcat (min^-1)' = 1.1; column 'kcat/Km (uM^-1 min^-1)' = 0.0039; column 'Relative kcat/Km' = 0.006.

raw_value_unit_evidence: Table 2, Protein row 'F490A': Km = 274 uM; kcat = 1.1 min^-1; printed kcat/Km = 0.0039 uM^-1 min^-1.

row_label: Table 2, row F490A


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P23970 and applied mutation signature R106A to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: isochorismate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17109 and applied mutation signature R413K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 294.15 K; buffer 50 mM phosphate

column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'R413K'; substrate line 'Isochorismate'; column 'kcat (min^-1)' = 2.30 plus or minus 0.20; column 'KM' = 0.35 plus or minus 0.14 micromolar; column 'kcat/KM (M^-1 min^-1)' = 6.6 x 10^6.

raw_value_unit_evidence: Table 1, protein 'R413K', substrate line 'Isochorismate': kcat (min^-1) cell 2.30; KM cell 0.35 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 6.6 x 10^6.

substrate: isochorismate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17109 and applied mutation signature R395K to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'R395K'; substrate line 'alpha-Ketoglutarate'; column 'kcat (min^-1)' = 8.62 plus or minus 0.84; column 'KM' = 67 plus or minus 18 micromolar; column 'kcat/KM (M^-1 min^-1)' = 1.3 x 10^5.

raw_value_unit_evidence: Table 1, protein 'R395K', substrate line 'alpha-Ketoglutarate': kcat (min^-1) cell 8.62; KM cell 67 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 1.3 x 10^5.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P17109 FASTA via REST; fetched and residue-checked 2026-06-08 and applied mutation signature R395K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17109 and applied mutation signature R395A to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'R395A'; substrate line 'alpha-Ketoglutarate'; column 'kcat (min^-1)' = 1.07 plus or minus 0.06; column 'KM' = 29 plus or minus 8 micromolar; column 'kcat/KM (M^-1 min^-1)' = 3.7 x 10^4.

raw_value_unit_evidence: Table 1, protein 'R395A', substrate line 'alpha-Ketoglutarate': kcat (min^-1) cell 1.07; KM cell 29 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 3.7 x 10^4.


sequence_source: UniProtKB reviewed P17109 FASTA via REST; fetched and residue-checked 2026-06-08


column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'R413K'; substrate line 'alpha-Ketoglutarate'; column 'kcat (min^-1)' = 2.57 plus or minus 0.31; column 'KM' = 115 plus or minus 37 micromolar; column 'kcat/KM (M^-1 min^-1)' = 2.2 x 10^4.

raw_value_unit_evidence: Table 1, protein 'R413K', substrate line 'alpha-Ketoglutarate': kcat (min^-1) cell 2.57; KM cell 115 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 2.2 x 10^4.


substrate_name: 2-oxoglutarate; isochorismate

sequence_variant_note: Resolved canonical sequence from reconstructed from direct UniProtKB P17109 canonical sequence and applied mutation signature R395K to reconstruct the assayed variant sequence.

substrate: 2-oxoglutarate; isochorismate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17109 and applied mutation signature R395K/R413K to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'R395K/R413K'; substrate line 'alpha-Ketoglutarate'; column 'kcat (min^-1)' = 0.16 plus or minus 0.02; column 'KM' = 172 plus or minus 46 micromolar; column 'kcat/KM (M^-1 min^-1)' = 9.3 x 10^2.

raw_value_unit_evidence: Table 1, protein 'R395K/R413K', substrate line 'alpha-Ketoglutarate': kcat (min^-1) cell 0.16; KM cell 172 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 9.3 x 10^2.


sequence_variant_note: Resolved canonical sequence from reconstructed from direct UniProtKB P17109 canonical sequence and applied mutation signature R395K/R413K to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: direct UniProtKB P17109 canonical sequence

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

proof_lines:
Raw SKiD Env: Temp=21°C, pH=7
Raw SKiD Env: Temp=-----, pH=7.4

source: skid


substrate_name: 4-nitrophenyl beta-D-glucopyranoside; sinigrin; gluconasturtiin

sequence_source: direct UniProtKB I1TIJ2 canonical sequence

proof_lines:
pH 5.5, 37°C
recombinant enzyme, pH 5.5, 37°C


organism: Carica papaya

sequence_source: direct UniProtKB C9WCQ1 canonical sequence


sequence_source: direct UniProtKB C9WCQ0 canonical sequence

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P23970 (MEND_BACSU) REST FASTA/JSON; single-site alanine variant reconstructed after residue-position check; mutation family supported by PMID:20600129 / PMCID:PMC2914249. and applied mutation signature R409A to reconstruct the assayed variant sequence.


column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'L493A'; column 'Km (uM)' = 39; column 'kcat (min^-1)' = 19; column 'kcat/Km (uM^-1 min^-1)' = 0.49; column 'Relative kcat/Km' = 0.03.

raw_value_unit_evidence: Table 3, Protein row 'L493A': Km = 39 uM; kcat = 19 min^-1; printed kcat/Km = 0.49 uM^-1 min^-1.

row_label: Table 3, row L493A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature R106A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-state kinetic parameters with respect to alpha-ketoglutarate (2-oxoglutarate), Bacillus subtilis MenD; Protein row 'R106A'; column 'Km (uM)' = 7.7; column 'kcat (min^-1)' = 0.6; column 'kcat/Km (uM^-1 min^-1)' = 0.09; column 'Relative kcat/Km' = 0.1.

raw_value_unit_evidence: Table 2, Protein row 'R106A': Km = 7.7 uM; kcat = 0.6 min^-1; printed kcat/Km = 0.09 uM^-1 min^-1.

row_label: Table 2, row R106A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P23970 (MEND_BACSU) REST FASTA/JSON; single-site alanine variant reconstructed after residue-position check; mutation family supported by PMID:20600129 / PMCID:PMC2914249. and applied mutation signature I489A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature R428A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'R428A'; column 'Km (uM)' = 1.1; column 'kcat (min^-1)' = 2.8; column 'kcat/Km (uM^-1 min^-1)' = 2.8; column 'Relative kcat/Km' = 0.15.

raw_value_unit_evidence: Table 3, Protein row 'R428A': Km = 1.1 uM; kcat = 2.8 min^-1; printed kcat/Km = 2.8 uM^-1 min^-1.

row_label: Table 3, row R428A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P23970 (MEND_BACSU) REST FASTA/JSON; single-site alanine variant reconstructed after residue-position check; mutation family supported by PMID:20600129 / PMCID:PMC2914249. and applied mutation signature L493A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P23970 (MEND_BACSU) REST FASTA/JSON; single-site alanine variant reconstructed after residue-position check; mutation family supported by PMID:20600129 / PMCID:PMC2914249. and applied mutation signature R428A to reconstruct the assayed variant sequence.


column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'R106A'; column 'Km (uM)' = 41; column 'kcat (min^-1)' = 0.7; column 'kcat/Km (uM^-1 min^-1)' = 0.018; column 'Relative kcat/Km' = 0.00095.

raw_value_unit_evidence: Table 3, Protein row 'R106A': Km = 41 uM; kcat = 0.7 min^-1; printed kcat/Km = 0.018 uM^-1 min^-1.

row_label: Table 3, row R106A


sequence_source: UniProtKB reviewed accession P23970 direct REST lookup on 2026-06-08

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'Wild type'; column 'Km (uM)' = 1.1; column 'kcat (min^-1)' = 19; column 'kcat/Km (uM^-1 min^-1)' = 19; column 'Relative kcat/Km' = 1.

raw_value_unit_evidence: Table 3, Protein row 'Wild type': Km = 1.1 uM; kcat = 19 min^-1; printed kcat/Km = 19 uM^-1 min^-1.

row_label: Table 3, row Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23970 and applied mutation signature K299A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters with respect to isochorismate, Bacillus subtilis MenD; Protein row 'K299A'; column 'Km (uM)' = 8.4; column 'kcat (min^-1)' = 25; column 'kcat/Km (uM^-1 min^-1)' = 3.0; column 'Relative kcat/Km' = 0.16.

raw_value_unit_evidence: Table 3, Protein row 'K299A': Km = 8.4 uM; kcat = 25 min^-1; printed kcat/Km = 3.0 uM^-1 min^-1.

row_label: Table 3, row K299A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P23970 direct REST lookup on 2026-06-08; row mutation K299A reconstructed from canonical sequence and applied mutation signature K299A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P17109 direct REST lookup on 2026-06-08

column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'WT'; substrate line 'alpha-Ketoglutarate'; column 'kcat (min^-1)' = 17.2 plus or minus 1.5; column 'KM' = 2.9 plus or minus 1.3 micromolar; column 'kcat/KM (M^-1 min^-1)' = 5.9 x 10^6.

raw_value_unit_evidence: Table 1, protein 'WT', substrate line 'alpha-Ketoglutarate': kcat (min^-1) cell 17.2; KM cell 2.9 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 5.9 x 10^6.


column_label: Table 1: Steady-state kinetic parameters of MenD and its mutants (Biochemical Journal 2018, volume 475, pages 3651-3667); protein row 'R395A'; substrate line 'Isochorismate'; column 'kcat (min^-1)' = 3.91 plus or minus 0.08; column 'KM' = 16 plus or minus 1 micromolar; column 'kcat/KM (M^-1 min^-1)' = 2.4 x 10^5.

raw_value_unit_evidence: Table 1, protein 'R395A', substrate line 'Isochorismate': kcat (min^-1) cell 3.91; KM cell 16 in the micromolar unit the Methods state for that constant; kcat/KM (M^-1 min^-1) cell 2.4 x 10^5.


organism: Citrobacter sp. Wye1


organism: Homo sapiens

substrate_name: D-glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed Q96EK6 after direct residue check on 2026-06-08. and applied mutation signature E156A to reconstruct the assayed variant sequence.

substrate: D-glucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed Q96EK6 after direct residue check on 2026-06-08. and applied mutation signature E156D to reconstruct the assayed variant sequence.


substrate_name: propionyl-CoA

assay_conditions_summary: pH 7.6; 310.15 K; cofactor CoA

proof_lines:
pH 7.6, 37°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.6

substrate: propionyl-CoA


organism: Mus musculus

assay_conditions_summary: cofactor CoA


organism: Plasmodium falciparum

substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


organism: Arabidopsis thaliana

substrate_name: acetyl-coenzyme A

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

substrate: acetyl-coenzyme A


organism: Oryza sativa subsp. japonica


organism: Trypanosoma brucei brucei

substrate_name: glucosamine 6-phosphate (at pH 7.2 and room temperature)

assay_conditions_summary: pH 7.2; cofactor CoA


organism: Mycobacterium tuberculosis

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


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


substrate_name: Unknown

substrate: Unknown


proof_lines: mutant R293K, pH 7.4, temperature not specified in the publication


proof_lines: mutant E55D, pH 7.4, temperature not specified in the publication


proof_lines: mutant K292Q, pH 7.4, temperature not specified in the publication


proof_lines: mutant R413K, pH 7.4, temperature not specified in the publication


proof_lines: mutant S391A, pH 7.4, temperature not specified in the publication


proof_lines: wild-type, pH 7.4, temperature not specified in the publication


substrate_name: 2-Oxoglutarate; Isochorismate

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_rest:P23970 and applied mutation signature K299A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD K299A

substrate: 2-Oxoglutarate; Isochorismate


substrate_name: Isochorismate; 2-Oxoglutarate

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

substrate: Isochorismate; 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_rest:P17109 and applied mutation signature R395A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_rest:P17109 and applied mutation signature R413K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_rest:P17109 and applied mutation signature R395K/R413K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R395K/R413K, at pH 7.0 and 21°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_rest:P17109 and applied mutation signature R395K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature R32A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD R32A


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature F490A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD F490A


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature R106A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD R106A


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature R409A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD R409A


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature I489A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD I489A


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature L493A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD L493A


sequence_variant_note: Resolved canonical sequence from UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present and applied mutation signature R428A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase(Enzyme) mutant MenD R428A


sequence_source: UniProtKB P23970 direct REST/FASTA check; variant sequence reconstructed from the canonical sequence when mutation_signature is present

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


sequence_source: UniProtKB:P17109 MEND_ECOLI canonical sequence fetched by direct UniProt REST check

proof_lines: pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17109 canonical sequence with R395K reconstructed from the selected BRENDA mutation note and applied mutation signature R395K to reconstruct the assayed variant sequence.

proof_lines: mutant R395K, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17109 canonical sequence with I418L reconstructed from the selected BRENDA mutation note and applied mutation signature I418L to reconstruct the assayed variant sequence.

proof_lines: mutant I418L, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17109 canonical sequence with R107K reconstructed from the selected BRENDA mutation note and applied mutation signature R107K to reconstruct the assayed variant sequence.

proof_lines: mutant R107K, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17109 canonical sequence with S32A reconstructed from the selected BRENDA mutation note and applied mutation signature S32A to reconstruct the assayed variant sequence.

proof_lines: mutant S32A, pH 7.4, temperature not specified in the publication


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

proof_lines: mutant R292Q, pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB REST FASTA Q9LFU9

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

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


organism: Aspergillus fumigatus

substrate_name: D-Glucosamine 6-phosphate; Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA Q4WCU5 plus direct G183E substitution and applied mutation signature G183E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant G183E

substrate: D-Glucosamine 6-phosphate; Acetyl-CoA


substrate_name: D-Glucosamine 6-phosphate

sequence_source: UniProtKB REST FASTA Q4WCU5 plus direct G183E substitution

substrate: D-Glucosamine 6-phosphate


substrate_name: Acetyl-CoA

sequence_source: UniProtKB REST FASTA Q4WCU5

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1'; column 'K m AcCoA' = 40 uM; column 'k cat' = 38 s-1; column 'k cat /K m AcCoA' = 0.95 s-1 uM-1. The row's other columns, 'K m GlcN-6P' and 'k cat /K m GlcN-6P', belong to the D-glucosamine 6-phosphate axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 38 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 38.0 s^(-1). Km: printed Table 2 cell 40 uM; 40 / 1000 = 0.04 mM; the paper value is 0.04 mM. kcat/Km: printed Table 2 cell 0.95 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.95 x 1000 = 950.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1': K m AcCoA = 40 uM; k cat = 38 s-1; printed k cat /K m AcCoA = 0.95 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1', AcCoA columns

substrate: Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA Q4WCU5 plus direct V125R substitution and applied mutation signature V125R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant V125R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4WCU5 and applied mutation signature E185Y to reconstruct the assayed variant sequence.

column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1-E185Y'; column 'K m GlcN-6P' = 30 uM; column 'k cat' = 1.3 s-1; column 'k cat /K m GlcN-6P' = 0.042 s-1 uM-1. The row's other columns, 'K m AcCoA' and 'k cat /K m AcCoA', belong to the acetyl-CoA axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.3 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 1.3 s^(-1). Km: printed Table 2 cell 30 uM; 30 / 1000 = 0.03 mM; the paper value is 0.03 mM. kcat/Km: printed Table 2 cell 0.042 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.042 x 1000 = 42.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1-E185Y': K m GlcN-6P = 30 uM; k cat = 1.3 s-1; printed k cat /K m GlcN-6P = 0.042 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1-E185Y', GlcN-6P columns


substrate_name: Acetyl-CoA; D-Glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA Q4WCU5 plus direct E185Y substitution and applied mutation signature E185Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant E185Y

substrate: Acetyl-CoA; D-Glucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4WCU5 and applied mutation signature V125R to reconstruct the assayed variant sequence.

column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1-V125R'; column 'K m AcCoA' = 200 uM; column 'k cat' = 0.12 s-1; column 'k cat /K m AcCoA' = 0.00058 s-1 uM-1. The row's other columns, 'K m GlcN-6P' and 'k cat /K m GlcN-6P', belong to the D-glucosamine 6-phosphate axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.12 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.12 s^(-1). Km: printed Table 2 cell 200 uM; 200 / 1000 = 0.2 mM; the paper value is 0.2 mM. kcat/Km: printed Table 2 cell 0.00058 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00058 x 1000 = 0.58 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1-V125R': K m AcCoA = 200 uM; k cat = 0.12 s-1; printed k cat /K m AcCoA = 0.00058 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1-V125R', AcCoA columns


column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1-E185Y'; column 'K m AcCoA' = 40 uM; column 'k cat' = 1.3 s-1; column 'k cat /K m AcCoA' = 0.031 s-1 uM-1. The row's other columns, 'K m GlcN-6P' and 'k cat /K m GlcN-6P', belong to the D-glucosamine 6-phosphate axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.3 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 1.3 s^(-1). Km: printed Table 2 cell 40 uM; 40 / 1000 = 0.04 mM; the paper value is 0.04 mM. kcat/Km: printed Table 2 cell 0.031 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.031 x 1000 = 31.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1-E185Y': K m AcCoA = 40 uM; k cat = 1.3 s-1; printed k cat /K m AcCoA = 0.031 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1-E185Y', AcCoA columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4WCU5 FASTA; Y189R reconstructed from the selected mutation_signature after confirming canonical residue 189 is Y. and applied mutation signature Y189R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q4WCU5 FASTA; source row is marked wild_type and the RCSB 2VXK entity aligns to Q4WCU5 over residues 1-190.

column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1'; column 'K m GlcN-6P' = 71 uM; column 'k cat' = 38 s-1; column 'k cat /K m GlcN-6P' = 0.53 s-1 uM-1. The row's other columns, 'K m AcCoA' and 'k cat /K m AcCoA', belong to the acetyl-CoA axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 38 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 38.0 s^(-1). Km: printed Table 2 cell 71 uM; 71 / 1000 = 0.071 mM; the paper value is 0.071 mM. kcat/Km: printed Table 2 cell 0.53 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.53 x 1000 = 530.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1': K m GlcN-6P = 71 uM; k cat = 38 s-1; printed k cat /K m GlcN-6P = 0.53 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1', GlcN-6P columns


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 Q4WCU5 FASTA; Y189R reconstructed from the selected mutation_signature and SABIO-RK modifier note after confirming canonical residue 189 is Y. and applied mutation signature Y189R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant Y189R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4WCU5 and applied mutation signature Y189R to reconstruct the assayed variant sequence.

column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1-Y189R'; column 'K m AcCoA' = 86 uM; column 'k cat' = 1.7 s-1; column 'k cat /K m AcCoA' = 0.019 s-1 uM-1. The row's other columns, 'K m GlcN-6P' and 'k cat /K m GlcN-6P', belong to the D-glucosamine 6-phosphate axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.7 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 1.7 s^(-1). Km: printed Table 2 cell 86 uM; 86 / 1000 = 0.086 mM; the paper value is 0.086 mM. kcat/Km: printed Table 2 cell 0.019 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.019 x 1000 = 19.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1-Y189R': K m AcCoA = 86 uM; k cat = 1.7 s-1; printed k cat /K m AcCoA = 0.019 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1-Y189R', AcCoA columns


column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Af GNA1-V125R'; column 'K m GlcN-6P' = 600 uM; column 'k cat' = 0.12 s-1; column 'k cat /K m GlcN-6P' = 0.00019 s-1 uM-1. The row's other columns, 'K m AcCoA' and 'k cat /K m AcCoA', belong to the acetyl-CoA axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.12 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.12 s^(-1). Km: printed Table 2 cell 600 uM; 600 / 1000 = 0.6 mM; the paper value is 0.6 mM. kcat/Km: printed Table 2 cell 0.00019 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00019 x 1000 = 0.19 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Af GNA1-V125R': K m GlcN-6P = 600 uM; k cat = 0.12 s-1; printed k cat /K m GlcN-6P = 0.00019 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Af GNA1-V125R', GlcN-6P columns


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 and applied mutation signature L119A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 and applied mutation signature G112A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant G112A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 and applied mutation signature F142A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 and applied mutation signature G147A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant L119A


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:P43577 and applied mutation signature E98A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature I116A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant I116A


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature I97A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant I97A


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature G112A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature Q107A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant Q107A


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature G147A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant G147A


sequence_source: UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature L115A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant L115A


sequence_variant_note: Resolved canonical sequence from UniProtKB P43577 canonical sequence fetched 2026-06-08; variant reconstructed from selected mutation_signature and applied mutation signature V102A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant V102A


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

proof_lines:
isoenzyme 3
isoenzyme 1
isoenzymes 2 and 3


sequence_source: UniProtKB REST Q96EK6 direct lookup on 2026-06-08


proof_lines:
pH 7.6, 37°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.6


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q96EK6 direct lookup plus E156A substitution reconstruction on 2026-06-08 and applied mutation signature E156A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant E156A


sequence_source: UniProtKB REST Q96EK6 direct lookup plus E156A substitution reconstruction on 2026-06-08


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q96EK6 direct lookup plus E156D substitution reconstruction on 2026-06-08 and applied mutation signature E156D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant E156D


sequence_source: UniProtKB REST Q96EK6 direct lookup plus E156D substitution reconstruction on 2026-06-08


sequence_source: UniProtKB REST Q9JK38 direct lookup on 2026-06-08


organism: Neurospora crassa

sequence_source: UniProtKB REST Q7SHA4 direct lookup on 2026-06-08


organism: Oryza sativa

sequence_source: UniProtKB Q5U9F2 direct REST lookup


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: pH 7.2; 296.15 K; cofactor CoA


sequence_source: UniProtKB C6KTC5 direct REST lookup


sequence_variant_note: Resolved canonical sequence from Reconstructed V102A variant from UniProtKB P43577 canonical sequence and applied mutation signature V102A to reconstruct the assayed variant sequence.


organism: Caenorhabditis elegans


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Q155V/C158G to reconstruct the assayed variant sequence.


organism: Cryptosporidium parvum

source_db: mixed

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

source: mixed


column_label: Table 2: Comparison of the kinetic parameters between the human and the fungal enzyme and the corresponding mutations (Biochem. J. 2008, 415(2):217-223), enzyme-form row 'Hs GNA1'; column 'K m AcCoA' = 26 uM; column 'k cat' = 9 s-1; column 'k cat /K m AcCoA' = 0.34 s-1 uM-1. The row's other columns, 'K m GlcN-6P' and 'k cat /K m GlcN-6P', belong to the D-glucosamine 6-phosphate axis of the same enzyme form.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 9.0 s^(-1). Km: printed Table 2 cell 26 uM; 26 / 1000 = 0.026 mM; the paper value is 0.026 mM. kcat/Km: printed Table 2 cell 0.34 s-1 uM-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.34 x 1000 = 340.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'Hs GNA1': K m AcCoA = 26 uM; k cat = 9 s-1; printed k cat /K m AcCoA = 0.34 s-1 uM-1. The table sub-caption gives the units of the three columns as uM, s-1 and s-1 uM-1 and states that all of the parameters were obtained at pH 7.5.

row_label: Table 2, enzyme-form row 'Hs GNA1', AcCoA columns


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 FASTA direct check; F142A reconstructed from canonical GNA1 sequence and applied mutation signature F142A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant F142A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 FASTA direct check; Q107A reconstructed from canonical GNA1 sequence and applied mutation signature Q107A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 FASTA direct check; E98A reconstructed from canonical GNA1 sequence and applied mutation signature E98A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosamine-phosphate N-acetyltransferase(Enzyme) mutant E98A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 FASTA direct check; L115A reconstructed from canonical GNA1 sequence and applied mutation signature L115A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43577 FASTA direct check; I97A reconstructed from canonical GNA1 sequence and applied mutation signature I97A to reconstruct the assayed variant sequence.


organism: Ovis aries


organism: Rattus norvegicus


organism: Sus scrofa


organism: Vigna radiata var. radiata


organism: Aedes aegypti

sequence_source: UniProt Q5Q126; EMBL AY791896/AAV84018.1; PubMed-linked title PMID 15857769

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


substrate_name: glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q4WCU5 / RCSB PDB 2VEZ canonical sequence; source note mutant Y174F and applied mutation signature Y174F to reconstruct the assayed variant sequence.

substrate: glucosamine 6-phosphate


sequence_source: UniProt Q4WCU5; RCSB PDB 2VEZ; PMID 18005663


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q4WCU5 / RCSB PDB 2VXK canonical sequence; source note mutant E185Y and applied mutation signature E185Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q4WCU5 / RCSB PDB 2VXK canonical sequence; source note mutant Y189R and applied mutation signature Y189R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q4WCU5 / RCSB PDB 2VXK canonical sequence; source note mutant G183E and applied mutation signature G183E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q4WCU5 canonical sequence, anchored by UniProt reference PMID 18601654 and RCSB/PDB 2VXK; V125R applied by direct residue check. and applied mutation signature V125R to reconstruct the assayed variant sequence.


sequence_source: UniProt Q4WCU5 canonical wild-type sequence, anchored by UniProt reference PMID 18601654 and RCSB/PDB 2VXK.


organism: Blastocladiella emersonii

substrate_name: coenzyme A

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

substrate: coenzyme A


sequence_source: Reviewed UniProt Q5U9F2/GNA1 sequence, anchored by lead PMID 15849305.


enzyme_display_name: amylosucrase

organism: Neisseria polysaccharea

substrate_name: sucrose (in the sucrose consumption assay, when initial sucrose < 20 mM)

proof_lines: This enzyme does not present a classic Michaelis-Menten behavior for sucrose consumption, that could be related to the presence of a second sucrose binding site. Nevertheless, it is possible to model sucrose consumption rate versus sucrose

enzyme: amylosucrase


organism: Xanthomonas campestris pv. campestris

substrate_name: hydroquinone

sequence_source: UniProtKB A0A0H2X5U3 FASTA direct lookup

substrate: hydroquinone


substrate_name: Sucrose; H2O

sequence_source: UniProt Q9ZEU2 parent accession checked, but row-specific variant sequence unresolved

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

proof_lines: SABIO-RK modifier species: amylosucrase(Enzyme) mutant 001-D2

proof_lines: SABIO-RK modifier species: amylosucrase(Enzyme) mutant 002-G1

substrate: Sucrose; H2O


substrate_name: sucrose

sequence_variant_note: Resolved canonical sequence from UniProt Q9ZEU2 canonical sequence with selected source mutation signature applied at computed +8 UniProt coordinate offset and applied mutation signature R226L/I228V/F229A/A289I/F290Y/E300I/V331T with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

substrate: sucrose


sequence_variant_note: Resolved canonical sequence from UniProt Q9ZEU2 canonical sequence with selected source mutation signature applied at computed +8 UniProt coordinate offset and applied mutation signature R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9ZEU2 canonical sequence with selected source mutation signature applied at computed +8 UniProt coordinate offset and applied mutation signature R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_source: UniProt Q9ZEU2 canonical sequence with selected source mutation signature applied at computed +8 UniProt coordinate offset


sequence_variant_note: Resolved canonical sequence from UniProt Q9ZEU2 canonical sequence with selected source mutation signature applied at computed +8 UniProt coordinate offset and applied mutation signature R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_source: UniProt Q9ZEU2 canonical sequence from direct UniProt REST check and accession reuse cache


organism: Deinococcus geothermalis

sequence_source: UniProtKB REST direct accession lookup for Q1J0W0 on 2026-06-08


proof_lines:
pH 7.0, 45°C
pH 5.0, 45°C
Raw SKiD Env: Temp=45°C, pH=7


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

proof_lines: 45°C, pH not specified in the publication, wild-type enzyme, critical sucrose concentration above 84 mM, total activity (hydrolysis and polymerization)

proof_lines: 45°C, pH not specified in the publication, wild-type enzyme, critical sucrose concentration below 84 mM, total activity (hydrolysis and polymerization)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q1J0W0 on 2026-06-08 and applied mutation signature A226N to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme A226N


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q1J0W0 on 2026-06-08 and applied mutation signature R30A to reconstruct the assayed variant sequence.

proof_lines: 45°C, pH not specified in the publication, mutant enzyme R30A, critical sucrose concentration below 84 mM, total activity (hydrolysis and polymerization)

proof_lines: 45°C, pH not specified in the publication, mutant enzyme R30A, critical sucrose concentration above 84 mM, total activity (hydrolysis and polymerization)


sequence_source: UniProtKB REST direct accession lookup for Q9ZEU2 on 2026-06-08


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----


organism: Bergeriella denitrificans

sequence_source: UniProtKB A0A378UJ51, direct exact query for EC 2.4.1.4 and Bergeriella denitrificans


organism: Bifidobacterium thermophilum

proof_lines: mutant enzyme Y414F/P200R, sucrose concentration less than 89.7 mM, pH and temperature not specified in the publication

proof_lines: mutant enzyme Y414F/P200R, sucrose concentration above 89.7 mM, pH and temperature not specified in the publication


substrate_name: fructose

substrate: fructose


proof_lines: wild-type enzyme, sucrose concentration less than 89.7 mM, pH and temperature not specified in the publication

proof_lines: wild-type enzyme, sucrose concentration above 89.7 mM, pH and temperature not specified in the publication


organism: Calidithermus terrae

sequence_source: UniProtKB A0A399ELX4, direct exact query for EC 2.4.1.4 and Calidithermus terrae

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Deinococcus radiodurans

substrate_name: H2O; Sucrose

sequence_source: NCBI Protein NP_294657.1 and UniProtKB Q9RVT9, paper-linked DRAS locus in PMID 15733849

substrate: H2O; Sucrose


organism: Moraxella cuniculi


organism: Neisseria canis


organism: Neisseria cinerea


organism: Neisseria perflava


sequence_source: UniProtKB reviewed Q9ZEU2 (AMYS_NEIPO), Amylosucrase, Neisseria polysaccharea, EC 2.4.1.4

proof_lines: initial sucrose concentration lower than 20 mM, sucrose consumption

proof_lines: initial sucrose concentration higher than 20 mM, sucrose hydrolysis

proof_lines: initial sucrose concentration lower than 20 mM, polymerization


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

proof_lines: with maltotetraose, pH 7.0, 30°C, recombinant mutant R226N

proof_lines: with maltotriose, pH 7.0, 30°C, recombinant mutant R226N


proof_lines: with maltobiose, pH 7.0, 30°C, recombinant wild-type enzyme

proof_lines: with maltotriose, pH 7.0, 30°C, recombinant wild-type enzyme


organism: Neisseria sicca


organism: Neisseria subflava


enzyme_display_name: protein-synthesizing GTPase

organism: Homo sapiens

proof_lines: Obtained in the presence of 40S and 60S ribosomal subunits. 60S ribosomal subunit is necessary for enzyme activation, while 40S ribosomal subunit is not.

enzyme: protein-synthesizing GTPase


organism: Saccharolobus solfataricus

substrate_name: GTP

substrate: GTP


organism: Unknown


mutation_signature: truncated mutant

proof_lines: truncated mutant, domain G, 60°C, pH 7.8

proof_lines: truncated mutant, domains G+M, 60°C, pH 7.8


proof_lines: wild-type, pH 7.5, 60°C, presence of 40% ethylene glycol

proof_lines: wild-type, pH 7.5, 60°C, presence of 10% ethylene glycol


organism: Saccharomyces pastorianus

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Schizosaccharomyces pombe


sequence_source: UniProtKB Q980A5 direct lookup; reviewed Swiss-Prot entry IF2G_SACS2.

proof_lines:
Raw SKiD Env: Temp=60°C, pH=-----
Raw SKiD Env: Temp=50°C, pH=7.8
Raw SKiD Env: Temp=75°C, pH=7.8


organism: Sulfolobus solfataricus

substrate_name: GTP; H2O

proof_lines: SABIO-RK modifier species: protein-synthesizing GTPase(Enzyme) mutant T213V C-terminal His-tag

substrate: GTP; H2O


sequence_source: UniProtKB Q980M3 direct lookup; reviewed Swiss-Prot entry HFLX_SACS2.


proof_lines: SABIO-RK modifier species: protein-synthesizing GTPase(Enzyme) mutant F236P C-terminal His-tag


organism: Escherichia coli


proof_lines: mutant A26G, pH 7.5, 60°C, presence of 10% ethylene glycol

proof_lines: mutant A26G, pH 7.5, 60°C, presence of 40% ethylene glycol


sequence_source: UniProtKB reviewed accession P35021


mutation_signature: N-terminal deletion mutant

proof_lines: pH 7.8, 50°C, N-terminal deletion mutant


proof_lines:
pH 7.4, 50°C, in absence of ribosomes
pH 7.8, 50°C, full-length enzyme
Raw SKiD Env: Temp=50°C, pH=7.5


sequence_source: UniProtKB reviewed accession P60785 direct lookup on 2026-06-08

proof_lines: recombinant wild-type enzyme in absence of 70S ribosome, pH 7.5, 37°C

proof_lines: recombinant wild-type enzyme in presence of 70S ribosome, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6M8 direct lookup on 2026-06-08; variant reconstructed from selected mutation label and PMID 26264741 mature-chain numbering and applied mutation signature H91A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: in presence of 70S ribosome, H91A, pH 7.5, 37°C

proof_lines: recombinant enzyme EF-G mutant H91A, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6M8 direct lookup on 2026-06-08; variant reconstructed from selected mutation label and PMID 26264741 mature-chain numbering and applied mutation signature H91R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: in presence of 70S ribosome, H91R, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6M8 direct lookup on 2026-06-08; variant reconstructed from selected mutation label and PMID 26264741 mature-chain numbering and applied mutation signature F94L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: in presence of 70S ribosome, F94L, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6M8 direct lookup on 2026-06-08; variant reconstructed from selected mutation label and PMID 26264741 mature-chain numbering and applied mutation signature H91Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: in presence of 70S ribosome, H91Q, pH 7.5, 37°C


sequence_source: UniProtKB reviewed accession P0A6M8 direct lookup on 2026-06-08

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

proof_lines: in presence of 70S ribosome, wild-type enzyme, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6M8 direct lookup on 2026-06-08; variant reconstructed from selected mutation label and PMID 26264741 mature-chain numbering and applied mutation signature H91E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: in presence of 70S ribosome, H91E, pH 7.5, 37°C


enzyme_display_name: phospholipase C

organism: Bacillus cereus

proof_lines:
wild type enzyme, at pH 7.0 and 50°C
monomeric substrate, wild-type PLC
micellar substrate, wild-type PLC

enzyme: phospholipase C


substrate_name: diheptanoylphosphatidylcholine

proof_lines:
micellar substrate, recombinant PLC
monomeric substrate, recombinant PLC
water-soluble substrate

substrate: diheptanoylphosphatidylcholine


organism: Clostridium perfringens

substrate_name: sphingomyelin

substrate: sphingomyelin


organism: Legionella pneumophila

substrate_name: p-Nitrophenylphosphorylcholine

substrate: p-Nitrophenylphosphorylcholine


substrate_name: Phosphatidylcholine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature E4Q/Y56T with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4Q/Y56T

substrate: Phosphatidylcholine; H2O


substrate_name: H2O; Phosphatidylcholine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature E4D/Y56D/F66N with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4D/Y56D/F66N

substrate: H2O; Phosphatidylcholine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature Y56L/F66L with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant Y56L/F66L


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature E4K with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature E4G/Y56I/F66N with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4G/Y56I/F66N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature F66Y with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant F66Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature E4Q/F66Y with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4Q/F66Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09598 direct REST/flat-file check; mature chain 39..283 used for mutation coordinate mapping and applied mutation signature E4G/Y56T/F66N with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4G/Y56T/F66N


sequence_variant_note: Resolved canonical sequence from UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39. and applied mutation signature E4Q/Y56T/F66Y with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4Q/Y56T/F66Y


sequence_variant_note: Resolved canonical sequence from UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39. and applied mutation signature E4R/Y56S/F66N with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4R/Y56S/F66N


sequence_variant_note: Resolved canonical sequence from UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39. and applied mutation signature Y56T/F66P with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant Y56T/F66P


sequence_variant_note: Resolved canonical sequence from UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39. and applied mutation signature Y56T/F66Y with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant Y56T/F66Y