sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40261 and applied mutation signature Y20A to reconstruct the assayed variant sequence.

column_label: Table 3: Enzyme Kinetics of hNNMT Proteins (Biochemistry 2011, 50, 7800-7808); row label column 'hNNMT' = 'Y20A'; column 'Km (mM)' under the sub-head 'NCA' = 6.3; column 'kcat (s-1)' = 0.031; column 'kcat /Km (s-1 mM-1 )' under the sub-head 'NCA' = 0.005; the second 'Km (mM)' column, under the sub-head 'AdoMet', and the second 'kcat /Km (s-1 mM-1 )' column, under the sub-head 'AdoMet', belong to the co-substrate S-adenosyl-L-methionine and are not used for this nicotinamide row.

normalized_value_unit_evidence: Km: printed Table 3 cell under the NCA sub-head is 6.3 mM; the printed unit is already mM, so no unit conversion applies, and the printed value carries into the export unit as 6.3 mM. kcat: printed Table 3 cell is 0.031 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 0.031 s^(-1), the same number. kcat/Km: printed Table 3 cell under the NCA sub-head is 0.005 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies, and the quotient of the paper's own two printed cells, 0.031 / 6.3, returns that same printed efficiency once rounded to the paper's precision.

raw_value_unit_evidence: Table 3, row Y20A: Km (NCA) = 6.3 mM; kcat = 0.031 s^-1; printed kcat/Km (NCA) = 0.005 s^-1 mM^-1. The prose of the Results section states the same Km for this row a second time: for Y20A the paper reports that Km (NCA) increased 60-fold over the tm-'wt' value of 0.105 mM, and 0.105 multiplied by 60 is 6.3.

row_label: Table 3, row Y20A, nicotinamide (NCA) columns


enzyme_display_name: nicotinamide N-methyltransferase

organism: Homo sapiens

substrate_name: nicotinamide

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40261 and applied mutation signature Y20F to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 3: Enzyme Kinetics of hNNMT Proteins (Biochemistry 2011, 50, 7800-7808); row label column 'hNNMT' = 'Y20F'; column 'Km (mM)' under the sub-head 'NCA' = 0.24; column 'kcat (s-1)' = 0.041; column 'kcat /Km (s-1 mM-1 )' under the sub-head 'NCA' = 0.17; the second 'Km (mM)' column, under the sub-head 'AdoMet', and the second 'kcat /Km (s-1 mM-1 )' column, under the sub-head 'AdoMet', belong to the co-substrate S-adenosyl-L-methionine and are not used for this nicotinamide row.

normalized_value_unit_evidence: Km: printed Table 3 cell under the NCA sub-head is 0.24 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 0.24 mM. kcat: printed Table 3 cell is 0.041 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 0.041 s^(-1). kcat/Km: printed Table 3 cell under the NCA sub-head is 0.17 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies. The exported ratio 0.17083333333333334 is the full-precision quotient of the same two printed cells, 0.041 / 0.24 = 0.17083333333333334, and rounding that quotient to the one printed by the paper gives 0.17, the printed cell itself.

raw_value_unit_evidence: Table 3, row Y20F: Km (NCA) = 0.24 mM; kcat = 0.041 s^-1; printed kcat/Km (NCA) = 0.17 s^-1 mM^-1.

row_label: Table 3, row Y20F, nicotinamide (NCA) columns

data_origin: experimental

enzyme: nicotinamide N-methyltransferase

substrate: nicotinamide

status: verified

source: oed


verification_status: unverified

mutation_signature: Unknown

sequence_source: UniProt P40261 canonical sequence

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

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40261 and applied mutation signature D197A to reconstruct the assayed variant sequence.

column_label: Table 3: Enzyme Kinetics of hNNMT Proteins (Biochemistry 2011, 50, 7800-7808); row label column 'hNNMT' = 'D197A'; column 'Km (mM)' under the sub-head 'NCA' = 11.8; column 'kcat (s-1)' = 0.036; column 'kcat /Km (s-1 mM-1 )' under the sub-head 'NCA' = 0.003; the second 'Km (mM)' column, under the sub-head 'AdoMet', and the second 'kcat /Km (s-1 mM-1 )' column, under the sub-head 'AdoMet', belong to the co-substrate S-adenosyl-L-methionine and are not used for this nicotinamide row.

normalized_value_unit_evidence: Km: printed Table 3 cell under the NCA sub-head is 11.8 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 11.8 mM. kcat: printed Table 3 cell is 0.036 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 0.036 s^(-1). kcat/Km: printed Table 3 cell under the NCA sub-head is 0.003 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies. The exported ratio 0.0030508474576271183 is the full-precision quotient of the same two printed cells, 0.036 / 11.8 = 0.0030508474576271183, and rounding that quotient to the one printed by the paper gives 0.003, the printed cell itself.

raw_value_unit_evidence: Table 3, row D197A: Km (NCA) = 11.8 mM; kcat = 0.036 s^-1; printed kcat/Km (NCA) = 0.003 s^-1 mM^-1.

row_label: Table 3, row D197A, nicotinamide (NCA) columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40261 and applied mutation signature K100A/E101A/E103A to reconstruct the assayed variant sequence.

column_label: Table 3: Enzyme Kinetics of hNNMT Proteins (Biochemistry 2011, 50, 7800-7808); row label column 'hNNMT' = 'tm-"wt"'; column 'Km (mM)' under the sub-head 'NCA' = 0.105; column 'kcat (s-1)' = 0.083; column 'kcat /Km (s-1 mM-1 )' under the sub-head 'NCA' = 0.8; the second 'Km (mM)' column, under the sub-head 'AdoMet', and the second 'kcat /Km (s-1 mM-1 )' column, under the sub-head 'AdoMet', belong to the co-substrate S-adenosyl-L-methionine and are not used for this nicotinamide row.

normalized_value_unit_evidence: Km: printed Table 3 cell under the NCA sub-head is 0.105 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 0.105 mM. kcat: printed Table 3 cell is 0.083 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 0.083 s^(-1). kcat/Km: printed Table 3 cell under the NCA sub-head is 0.8 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies. The exported ratio 0.7904761904761906 is the full-precision quotient of the same two printed cells, 0.083 / 0.105 = 0.7904761904761906, and rounding that quotient to the one printed by the paper gives 0.8, the printed cell itself.

raw_value_unit_evidence: Table 3, row tm-"wt": Km (NCA) = 0.105 mM; kcat = 0.083 s^-1; printed kcat/Km (NCA) = 0.8 s^-1 mM^-1.

row_label: Table 3, row tm-"wt" (hNNMT K100A/E101A/E103A triple mutant), nicotinamide (NCA) columns


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProt P40261 canonical sequence with direct one-based mutation reconstruction and applied mutation signature Y20A to reconstruct the assayed variant sequence.

source: brenda


verification_status: corrected

sequence_source: UniProtKB:P40261 REST FASTA/JSON direct lookup on 2026-06-06

column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row '2-Methylpyridine'; column 'kcat (s-1)' = 0.01039; column 'Km (mM)' = 2.029; column 'kcat / Km (s-1 mM-1)' = 0.0051.

normalized_value_unit_evidence: kcat: printed cell 0.01039 s-1 -> 0.01039 s^(-1); the exported value is 0.01. Km: printed cell 2.029 mM -> 2.029 mM; the exported value is 2.029. kcat/Km: printed cell 0.0051 s-1 mM-1 -> 0.0051 s^(-1)*mM^(-1); the exported value is 0.004928536224741252.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row '2-Methylpyridine': kcat = 0.01039 s-1; Km = 2.029 mM; printed kcat / Km = 0.0051 s-1 mM-1.

status: corrected


substrate_name: nicotinimidamide

column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row 'Nicotinimidamide'; column 'kcat (s-1)' = 0.01350; column 'Km (mM)' = 1.326; column 'kcat / Km (s-1 mM-1)' = 0.0102.

normalized_value_unit_evidence: kcat: printed cell 0.01350 s-1 -> 0.0135 s^(-1); the exported value is 0.014. Km: printed cell 1.326 mM -> 1.326 mM; the exported value is 1.326. kcat/Km: printed cell 0.0102 s-1 mM-1 -> 0.0102 s^(-1)*mM^(-1); the exported value is 0.010558069381598792.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row 'Nicotinimidamide': kcat = 0.01350 s-1; Km = 1.326 mM; printed kcat / Km = 0.0102 s-1 mM-1.

substrate: nicotinimidamide


substrate_name: Isoquinoline

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

proof_lines: pH 7.5, temperature not specified in the publication

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

source_databases_merged: brenda skid

substrate: Isoquinoline


substrate_name: quinoline 3-carboxamide

column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row 'Quinoline-3-carboxamide'; column 'kcat (s-1)' = 0.00733; column 'Km (mM)' = 0.364; column 'kcat / Km (s-1 mM-1)' = 0.0201.

normalized_value_unit_evidence: kcat: printed cell 0.00733 s-1 -> 0.00733 s^(-1); the exported value is 0.007. Km: printed cell 0.364 mM -> 0.364 mM; the exported value is 0.364. kcat/Km: printed cell 0.0201 s-1 mM-1 -> 0.0201 s^(-1)*mM^(-1); the exported value is 0.019230769230769232.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row 'Quinoline-3-carboxamide': kcat = 0.00733 s-1; Km = 0.364 mM; printed kcat / Km = 0.0201 s-1 mM-1.

substrate: quinoline 3-carboxamide


column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row '3-Acetylpyridine'; column 'kcat (s-1)' = 0.01444; column 'Km (mM)' = 0.727; column 'kcat / Km (s-1 mM-1)' = 0.0199.

normalized_value_unit_evidence: kcat: printed cell 0.01444 s-1 -> 0.01444 s^(-1); the exported value is 0.014. Km: printed cell 0.727 mM -> 0.727 mM; the exported value is 0.727. kcat/Km: printed cell 0.0199 s-1 mM-1 -> 0.0199 s^(-1)*mM^(-1); the exported value is 0.01925722145804677.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row '3-Acetylpyridine': kcat = 0.01444 s-1; Km = 0.727 mM; printed kcat / Km = 0.0199 s-1 mM-1.


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: uridine/cytidine kinase

organism: Thermus thermophilus

substrate_name: cytidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5SKR5 REST FASTA/JSON direct lookup plus local Y93A substitution check on 2026-06-06 and applied mutation signature Y93A to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93A

enzyme: uridine/cytidine kinase

substrate: cytidine


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

proof_lines:
pH 7.2, 37°C, liver homogenate
recombinant protein


organism: Mus musculus

kcat_display: Not reported


organism: Oryctolagus cuniculus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Sus scrofa

substrate_name: Quinoline

substrate: Quinoline


organism: Acetivibrio thermocellus

substrate_name: cyclic 2',3'-AMP

sequence_variant_note: Resolved canonical sequence from NCBI Protein ZP_00312808.1 plus PMID:17986465 Table 1 D236A mutation evidence and applied mutation signature D236A to reconstruct the assayed variant sequence.

substrate: cyclic 2',3'-AMP


sequence_variant_note: Resolved canonical sequence from NCBI Protein ZP_00312808.1 plus PMID:17986465 Table 1 H189D mutation evidence and applied mutation signature H189D to reconstruct the assayed variant sequence.


enzyme_display_name: sterol 24-C-methyltransferase

organism: Saccharomyces cerevisiae

substrate_name: Zymosterol

sequence_source: UniProtKB reviewed accession P25087 (ERG6_YEAST), direct lookup for ERG6 in Saccharomyces cerevisiae S288c

enzyme: sterol 24-C-methyltransferase

substrate: Zymosterol


substrate_name: Zymosterol; S-Adenosyl-L-methionine

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

sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 direct REST FASTA/JSON lookup on 2026-06-06 and applied mutation signature E108L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant Glu108Leu

substrate: Zymosterol; S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 direct REST FASTA/JSON lookup on 2026-06-06 and applied mutation signature E209L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant Glu209Leu


substrate_name: S-Adenosyl-L-methionine; Zymosterol

sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 direct REST FASTA/JSON lookup on 2026-06-06 and applied mutation signature E246L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant Glu246Leu

substrate: S-Adenosyl-L-methionine; Zymosterol


sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 direct REST FASTA/JSON lookup on 2026-06-06 and applied mutation signature D189L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant Asp189Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 direct REST FASTA/JSON lookup on 2026-06-06 and applied mutation signature H107L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant His107Leu


substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProtKB P25087 direct REST FASTA/JSON lookup on 2026-06-06

substrate: S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40261; D197A reconstructed by substituting residue 197 D to A in the canonical sequence. and applied mutation signature D197A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P40261 canonical sequence.

proof_lines: 0.43-0.38 mM, wild type protein, pH 8.6, 37°C

proof_lines: 0.0018-0.0022 mM, wild type protein, pH 8.6, 37°C

proof_lines: 35-43 1/sec*mM, wild type protein, pH 8.6, 37°C


substrate_name: norharman

substrate: norharman


substrate_name: tetrahydroisoquinoline

column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row 'Tetrahydroisoquinoline'; column 'kcat (s-1)' = 0.04527; column 'Km (mM)' = 0.613; column 'kcat / Km (s-1 mM-1)' = 0.0739.

normalized_value_unit_evidence: kcat: printed cell 0.04527 s-1 -> 0.04527 s^(-1); the exported value is 0.045. Km: printed cell 0.613 mM -> 0.613 mM; the exported value is 0.613. kcat/Km: printed cell 0.0739 s-1 mM-1 -> 0.0739 s^(-1)*mM^(-1); the exported value is 0.0734094616639478.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row 'Tetrahydroisoquinoline': kcat = 0.04527 s-1; Km = 0.613 mM; printed kcat / Km = 0.0739 s-1 mM-1.

substrate: tetrahydroisoquinoline


column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row 'Isoquinoline'; column 'kcat (s-1)' = 0.01718; column 'Km (mM)' = 0.087; column 'kcat / Km (s-1 mM-1)' = 0.1975.

normalized_value_unit_evidence: kcat: printed cell 0.01718 s-1 -> 0.01718 s^(-1); the exported value is 0.017. Km: printed cell 0.087 mM -> 0.087 mM; the exported value is 0.087. kcat/Km: printed cell 0.1975 s-1 mM-1 -> 0.1975 s^(-1)*mM^(-1); the exported value is 0.19540229885057475.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row 'Isoquinoline': kcat = 0.01718 s-1; Km = 0.087 mM; printed kcat / Km = 0.1975 s-1 mM-1.


substrate_name: Thionicotinamide

column_label: Table 2. Kinetic parameters of confirmed NNMT substrates ranked according to their relative catalytic efficiency. Substrate row 'Thionicotinamide'; column 'kcat (s-1)' = 0.03336; column 'Km (mM)' = 0.111; column 'kcat / Km (s-1 mM-1)' = 0.3005.

normalized_value_unit_evidence: kcat: printed cell 0.03336 s-1 -> 0.03336 s^(-1); the exported value is 0.033. Km: printed cell 0.111 mM -> 0.111 mM; the exported value is 0.111. kcat/Km: printed cell 0.3005 s-1 mM-1 -> 0.3005 s^(-1)*mM^(-1); the exported value is 0.2972972972972973.

raw_value_unit_evidence: Table 2, decoded plain-numeral transcription (accepted manuscript page 16), substrate row 'Thionicotinamide': kcat = 0.03336 s-1; Km = 0.111 mM; printed kcat / Km = 0.3005 s-1 mM-1.

substrate: Thionicotinamide


organism: Chlamydomonas reinhardtii

substrate_name: 24(28)-methylene cycloartenol

sequence_source: UniProtKB A8IJ34 REST JSON, active TrEMBL entry for Chlamydomonas reinhardtii.

substrate: 24(28)-methylene cycloartenol


organism: Glycine max

substrate_name: Cycloartenol

sequence_source: UniProtKB Q43445 REST JSON, active TrEMBL entry for Glycine max.

substrate: Cycloartenol


substrate_name: 24-Methylene lophenol

substrate: 24-Methylene lophenol


sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 canonical sequence plus SABIO-RK mutant note; H238L reconstructed after confirming residue 238 is H. and applied mutation signature H238L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant His238Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 canonical sequence plus SABIO-RK mutant note; E224L reconstructed after confirming residue 224 is E. and applied mutation signature E224L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant Glu224Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB P25087 canonical sequence plus SABIO-RK mutant note; H199L reconstructed after confirming residue 199 is H. and applied mutation signature H199L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sterol 24-C-methyltransferase(Enzyme) mutant His199Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93E substitution and applied mutation signature Y93E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93E


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93M substitution and applied mutation signature Y93M to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93M


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93S substitution and applied mutation signature Y93S to reconstruct the assayed variant sequence.


substrate_name: uridine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93Q substitution and applied mutation signature Y93Q to reconstruct the assayed variant sequence.

substrate: uridine


sequence_source: UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93E substitution


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93I substitution and applied mutation signature Y93I to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93I


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence, reconstructed with paper-supported Y93W substitution and applied mutation signature Y93W to reconstruct the assayed variant sequence.


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


organism: Candida albicans

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

proof_lines:
pH 7.5, 30°C
versus S-adenosyl-L-methionine
versus sterol


organism: Candida tropicalis

substrate_name: desmosterol

proof_lines:
versus S-adenosyl-L-methionine
versus sterol

substrate: desmosterol


organism: Paracoccidioides brasiliensis

substrate_name: lanosterol

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, Vmax 2 pmol/min
pH 7.5, 37°C, Vmax: 50 pmol/min

substrate: lanosterol


organism: Pneumocystis carinii


organism: Trypanosoma brucei

proof_lines: mutant Y66F, pH not specified in the publication, 35°C


proof_lines: mutant Y177F, pH not specified in the publication, 35°C


proof_lines: mutant Y208F, pH not specified in the publication, 35°C


proof_lines: wild-type, pH not specified in the publication, 35°C


organism: Uromyces phaseoli

substrate_name: S-adenosyl-L-methionine; Zymosterol

proof_lines: value depends on concentration of detergent

substrate: S-adenosyl-L-methionine; Zymosterol


enzyme_display_name: ATP phosphoribosyltransferase

organism: Acinetobacter baumannii

substrate_name: ATP

sequence_source: UniProtKB A0A7U3XWM9 direct REST check on 2026-06-06

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: subunit HisGs, in the presence of Mn2+, at pH 7.5 and 25°C

proof_lines: full length enzyme, in the presence of Mg2+, at pH 7.5 and 25°C

enzyme: ATP phosphoribosyltransferase

substrate: ATP


organism: Arabidopsis thaliana

sequence_source: UniProtKB Q9S762 direct REST check on 2026-06-06

assay_conditions_summary: cofactor ATP

proof_lines:
recombinant enzyme
recombinant At-ATP-PRT1
crude cell extracts


mutation_signature: Δ1

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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: ATP phosphoribosyltransferase(Enzyme) wildtype AtATP-PRT2delta1-76, MBP fusion


proof_lines: SABIO-RK modifier species: ATP phosphoribosyltransferase(Enzyme) wildtype AtATP-PRT1delta1-74, MBP fusion


organism: Campylobacter jejuni

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB Q9PM78 direct REST check on 2026-06-06

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


proof_lines: with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25°C


sequence_source: UniProtKB Q5HSJ4 direct REST check on 2026-06-06

proof_lines: wild type long-form enzyme, at pH 8.5 and 25°C

proof_lines: wild type long-form enzyme , at pH 8.5 and 25°C


organism: Corynebacterium glutamicum

substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Z472 REST lookup 2026-06-06; variant reconstructed from selected mutation_signature S143F and applied mutation signature S143F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Z472 REST lookup 2026-06-06; variant reconstructed from selected mutation_signature S232Y/A270D and applied mutation signature S232Y/A270D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S232Y/A270D, at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Z472 REST lookup 2026-06-06; variant reconstructed from selected mutation_signature S232Y and applied mutation signature S232Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Z472 REST lookup 2026-06-06; variant reconstructed from selected mutation_signature A270D and applied mutation signature A270D to reconstruct the assayed variant sequence.


organism: Medicago truncatula

sequence_source: UniProtKB:G7JFL4 REST lookup 2026-06-06

assay_conditions_summary: pH 8; 297.15 K; cofactor ATP


proof_lines:
at pH 8.0 and 24°C
Raw SKiD Env: Temp=24°C, pH=8


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WMN1 REST lookup 2026-06-06


sequence_source: RCSB PDB 5UB9 polymer entity 1; UniProt Q5HSJ4 PDB chain range 1-225; PMID 29208762

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

mutation_type: truncation

proof_lines: truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProt Q5HSJ4 canonical reviewed sequence

source: skid


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q9Z472 canonical sequence using selected-row mutation signature and PMID 22172596 mutation context and applied mutation signature N215K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; cofactor ATP

proof_lines: N215K mutant protein, pH 8.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q9Z472 canonical sequence using selected-row mutation signature and PMID 22172596 mutation context and applied mutation signature L231F/T235A to reconstruct the assayed variant sequence.

proof_lines: L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q9Z472 canonical sequence using selected-row mutation signature and PMID 22172596 mutation context and applied mutation signature A270P to reconstruct the assayed variant sequence.

proof_lines: A270P mutant protein, pH 8.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q9Z472 canonical sequence using selected-row mutation signature and PMID 22172596 mutation context and applied mutation signature N215K/L231F/T235A to reconstruct the assayed variant sequence.

proof_lines: N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication


sequence_source: UniProt Q9Z472 canonical reviewed sequence

proof_lines: wild type protein, pH 8.5, temperature not specified in the publication


organism: Lactococcus lactis

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


proof_lines: Kii-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Acetivibrio thermocellus

substrate_name: cyclic 2',3'-AMP

substrate: cyclic 2',3'-AMP


organism: Saccharomyces cerevisiae


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: 26,27-dehydrozymosterol; Zymosterol

proof_lines:
versus zymosterol
versus S-adenosyl-L-methionine

substrate: 26,27-dehydrozymosterol; Zymosterol


substrate_name: Zymosterol; 26,27-dehydrozymosterol

substrate: Zymosterol; 26,27-dehydrozymosterol


organism: Psychrobacter arcticus

sequence_source: UniProtKB:Q4FQF7 direct accession lookup; canonical sequence retrieved 2026-06-06

assay_conditions_summary: pH 8.5; 283.15 K; cofactor ATP


assay_conditions_summary: pH 8.5; 288.15 K; cofactor ATP

proof_lines:
at pH 8.5 and 15°C
at pH 8.5 and 10°C
at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4FQF7 canonical sequence plus selected source mutation R32A; reconstructed 2026-06-06 and applied mutation signature R32A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 293.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4FQF7 canonical sequence plus selected source mutation R56A/K57A; reconstructed 2026-06-06 and applied mutation signature R56A/K57A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R56A/K57A, at pH 8.5 and 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4FQF7 canonical sequence plus selected source mutation R56A; reconstructed 2026-06-06 and applied mutation signature R56A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4FQF7 canonical sequence plus selected source mutation C115S; reconstructed 2026-06-06 and applied mutation signature C115S to reconstruct the assayed variant sequence.


substrate_name: cycloartenol

source_db: uniprot

substrate: cycloartenol

source: uniprot


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: zymosterol

substrate: zymosterol


protein_accession_database: NCBI Protein

sequence_variant_note: Resolved canonical sequence from ncbi_protein:ZP_00312808.1+single_substitution_reconstruction and applied mutation signature D392E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from ncbi_protein:ZP_00312808.1+single_substitution_reconstruction and applied mutation signature D236N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from ncbi_protein:ZP_00312808.1+single_substitution_reconstruction and applied mutation signature R237K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from ncbi_protein:ZP_00312808.1+single_substitution_reconstruction and applied mutation signature H376N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from ncbi_protein:ZP_00312808.1+single_substitution_reconstruction and applied mutation signature H189E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from ncbi_protein:ZP_00312808.1+single_substitution_reconstruction and applied mutation signature H323Q to reconstruct the assayed variant sequence.


substrate_name: AdoMet

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

substrate: AdoMet


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

proof_lines:
wild-type
pH 7.5, 32°C, wild-type enzyme
wild-type and mutant D79L


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


organism: Escherichia coli

substrate_name: sn-Glycerol 3-phosphate; Palmitoyl-CoA

sequence_source: UniProtKB:P0A7A7 FASTA direct lookup on 2026-06-06

assay_conditions_summary: cofactor CoA

substrate: sn-Glycerol 3-phosphate; Palmitoyl-CoA


organism: Helianthus annuus

substrate_name: stearoyl-[acyl-carrier protein]

sequence_source: UniProtKB:K9JTB0 FASTA direct lookup on 2026-06-06

smiles: *SC(=O)CCCCCCCCCCCCCCCCC

substrate: stearoyl-[acyl-carrier protein]


substrate_name: sn-glycerol 3-phosphate

substrate: sn-glycerol 3-phosphate


substrate_name: oleoyl-[acyl-carrier protein]

smiles: CCCCCCCCC=CCCCCCCCC(=O)S

substrate: oleoyl-[acyl-carrier protein]


smiles: O=P(O)(O)OCC(O)CO


substrate_name: palmitoyl-[acyl-carrier protein]

smiles: *SC(=O)CCCCCCCCCCCCCCC

substrate: palmitoyl-[acyl-carrier protein]


organism: Mus musculus

substrate_name: palmitoyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q61586 FASTA direct lookup on 2026-06-06 and applied mutation signature R318A to reconstruct the assayed variant sequence.

proof_lines: R318A mutant mitochondrial acyltransferase

substrate: palmitoyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q61586 FASTA direct lookup on 2026-06-06 and applied mutation signature R318K to reconstruct the assayed variant sequence.

proof_lines: R318K mutant mitochondrial acyltransferase


organism: Cucurbita moschata

sequence_source: UniProtKB reviewed accession P10349 direct REST lookup on 2026-06-06


sequence_source: UniProtKB reviewed accession P10349 direct REST lookup on 2026-06-06; variant sequence not reconstructed

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

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant isoform Q24a L261F


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7A7 canonical sequence plus row-specific E385R reconstruction on 2026-06-06 and applied mutation signature E385R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant E385R, C-terminal His6-tag


substrate_name: Palmitoyl-CoA; sn-Glycerol 3-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7A7 canonical sequence plus row-specific R354C reconstruction on 2026-06-06 and applied mutation signature R354C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant R354C, C-terminal His6-tag

substrate: Palmitoyl-CoA; sn-Glycerol 3-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7A7 canonical sequence plus row-specific G386A reconstruction on 2026-06-06 and applied mutation signature G386A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant G386A, C-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7A7 canonical sequence plus row-specific S308A reconstruction on 2026-06-06 and applied mutation signature S308A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant S308A, C-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7A7 canonical sequence plus row-specific G386L reconstruction on 2026-06-06 and applied mutation signature G386L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant G386L, C-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7A7 canonical sequence plus row-specific A349T reconstruction on 2026-06-06 and applied mutation signature A349T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant plsB26 (A349T)


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant I352A, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant P421S, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant F351A, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant S389A, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant H306G, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant D311G, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant R354K, C-terminal His6-tag


proof_lines: SABIO-RK modifier species: glycerol-3-phosphate O-acyltransferase(Enzyme) mutant


sequence_source: UniProtKB Q61586 / GPAT1_MOUSE direct accession lookup on 2026-06-06


sequence_source: UniProtKB O07807 / O07807_MYCTU direct accession lookup on 2026-06-06

assay_conditions_summary: 301.15 K; cofactor CoA

proof_lines: 28°C, pH not specified in the publication, cosubstrate: pamitoleoyl-CoA

proof_lines: 28°C, pH not specified in the publication, cosubstrate: oleoyl-CoA


organism: Rattus norvegicus

substrate_name: sn-Glycerol 3-phosphate; Myristoyl-CoA

sequence_source: UniProtKB P97564 / GPAT1_RAT direct accession lookup on 2026-06-06

substrate: sn-Glycerol 3-phosphate; Myristoyl-CoA


organism: Thermus thermophilus

substrate_name: cytidine

sequence_variant_note: Resolved canonical sequence from UniProt Q5SKR5 canonical sequence; Y93 substitution reconstructed during review and applied mutation signature Y93G to reconstruct the assayed variant sequence.

substrate: cytidine


sequence_variant_note: Resolved canonical sequence from UniProt Q5SKR5 canonical sequence; Y93 substitution reconstructed during review and applied mutation signature Y93M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SKR5 canonical sequence; Y93 substitution reconstructed during review and applied mutation signature Y93T to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93T


assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

proof_lines: pH 7.5, 22°C, isozyme mtGPAT1-knockout-mice mitochondria


organism: Unknown


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli (strain K12)


organism: Homo sapiens

substrate_name: 1-oleoyl-lysophosphatidic acid

substrate: 1-oleoyl-lysophosphatidic acid


enzyme_display_name: phosphoethanolamine N-methyltransferase

organism: Haemonchus contortus

substrate_name: phosphomonomethylethanolamine

proof_lines: isozyme PMT2, in 0.1 M HEPES (pH 8.0), 2 mM Na2EDTA, 10% glycerol, at 25°C

proof_lines: isozyme PMT1, in 0.1 M HEPES (pH 8.0), 2 mM Na2EDTA, 10% glycerol, at 25°C

enzyme: phosphoethanolamine N-methyltransferase

substrate: phosphomonomethylethanolamine


organism: Bursaphelenchus xylophilus

substrate_name: Ethanolamine phosphate

assay_conditions_summary: pH 8

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

substrate: Ethanolamine phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A1I7RPU0 and applied mutation signature Y127F to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant Y127F


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A1I7RPU0 and applied mutation signature M126I to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant M126I


organism: Caenorhabditis elegans

substrate_name: Phosphatidyl-N-methylethanolamine

substrate: Phosphatidyl-N-methylethanolamine


substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


substrate_name: phosphodimethylethanolamine

smiles: CN(C)CCOP(=O)(O)O

substrate: phosphodimethylethanolamine


organism: Chlamydomonas applanata

substrate_name: Phosphoethanolamine

proof_lines:
at pH 8.0 and 30°C
pH 8.0, 30°C

substrate: Phosphoethanolamine


organism: Chlamydomonas asymmetrica

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB A0A125SQH6 direct REST lookup, release 2026_01

proof_lines:
pH 8.0, 30°C
at pH 8.0 and 30°C

substrate: S-adenosyl-L-methionine


organism: Dictyocaulus viviparus

sequence_source: UniProtKB A0A0D8Y714 direct REST lookup, release 2026_01

proof_lines: pH 7.8, 22°C, recombinant His-tagged enzyme


sequence_source: UniProtKB U5HK46 direct REST lookup, release 2026_01


organism: Oesophagostomum dentatum

sequence_source: UniProtKB A0A0B1TAL6 direct REST lookup, release 2026_01


organism: Plasmodium falciparum

sequence_source: UniProtKB Q8IDQ9 direct REST lookup after Q6T755 inactive-merged redirect, release 2026_01

proof_lines: using phosphoethanolamine as cosubstrate pH and temperature not specified in the publication

proof_lines: using phosphodimethylethanolamine as cosubstrate, pH and temperature not specified in the publication


substrate_name: N,N-dimethylethanolamine phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8IDQ9 direct REST lookup after Q6T755 inactive-merged redirect; D128N reconstructed from selected mutation signature and applied mutation signature D128N to reconstruct the assayed variant sequence.

substrate: N,N-dimethylethanolamine phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8IDQ9 direct REST lookup after Q6T755 inactive-merged redirect; D128A reconstructed from selected mutation signature and applied mutation signature D128A to reconstruct the assayed variant sequence.


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


sequence_source: UniProtKB:Q8IDQ9 direct lookup; source accession Q6T755 is a secondary accession

smiles: NCCOP(=O)(O)O


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q8IDQ9 after direct D128 residue check; source accession Q6T755 is secondary and applied mutation signature D128N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q8IDQ9 after direct D128 residue check; source accession Q6T755 is secondary and applied mutation signature D128A to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB:Q8IDQ9 after direct D128 residue check; source accession Q6T755 is secondary


organism: Plasmodium knowlesi

sequence_source: UniProtKB:A0A384KJX3 direct lookup; source accession B3L8G9 is secondary/inactive

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


organism: Ancylostoma duodenale

sequence_source: UniProtKB REST direct accession lookup for A0A0C2DEB6, queried 2026-06-06


substrate_name: N-methylethanolamine phosphate

sequence_source: UniProtKB REST direct accession lookup for Q9C6B9, queried 2026-06-06

proof_lines: cosubstrate ethanolamine phosphate, pH 8.0, temperature not specified in the publication

proof_lines: cosubstrate N,N-dimethylethanolamine phosphate, pH 8.0, temperature not specified in the publication

substrate: N-methylethanolamine phosphate


sequence_source: UniProtKB REST direct accession lookup for Q9FR44, queried 2026-06-06

proof_lines: pH 8.0, temperature not specified in the publication


sequence_source: UniProtKB REST and flat-file direct accession lookup for Q944H0, queried 2026-06-06


sequence_variant_note: Resolved canonical sequence from UniProtKB REST canonical A0A1I7RPU0 plus direct H170A substitution reconstruction, queried 2026-06-06 and applied mutation signature H170A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant H170A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST canonical A0A1I7RPU0 plus direct S155A substitution reconstruction, queried 2026-06-06 and applied mutation signature S155A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant S155A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST canonical A0A1I7RPU0 plus direct T178V substitution reconstruction, queried 2026-06-06 and applied mutation signature T178V to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant T178V


sequence_variant_note: Resolved canonical sequence from UniProtKB REST canonical A0A1I7RPU0 plus direct S160A substitution reconstruction, queried 2026-06-06 and applied mutation signature S160A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant S160A


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_uniprot_Q5SKR5_PMID_28955773 and applied mutation signature Y93G to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93G


organism: Spinacia oleracea

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

proof_lines: SABIO-RK modifier species: phosphoethanolamine N-methyltransferase(Enzyme) mutant deltaPEAMT


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

sequence_source: UniProtKB Q9M571 FASTA direct lookup on 2026-06-06


organism: Toxocara canis

sequence_source: UniProtKB A0A0B2VTW9 FASTA direct lookup on 2026-06-06


organism: Triticum aestivum

sequence_source: UniProtKB Q8VYX1 FASTA direct lookup on 2026-06-06


organism: Thermus thermophilus

substrate_name: uridine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 FASTA direct lookup on 2026-06-06 plus selected mutation_signature Y93H and applied mutation signature Y93H to reconstruct the assayed variant sequence.

substrate: uridine


sequence_variant_note: Resolved canonical sequence from UniProt Q5SKR5 canonical sequence; Y93 substitution reconstructed during review and applied mutation signature Y93A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SKR5 canonical sequence; Y93 substitution reconstructed during review and applied mutation signature Y93N to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93N


sequence_source: UniProtKB Q5SKR5 FASTA direct lookup on 2026-06-06 plus selected mutation_signature Y93H


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: phosphoethanolamine

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

proof_lines: kcat is 109.0 min(-1) with phosphoethanolamine as substrate (PubMed:22117061, PubMed:25288796). kcat is 218.0 min(-1) with phospho-monomethylethanolamine as substrate (PubMed:22117061). kcat is 185.0 min(-1) with phospho-dimethylethanolamin

substrate: phosphoethanolamine


enzyme_display_name: glucan endo-1,3-beta-D-glucosidase

organism: Azumapecten farreri

substrate_name: Laminarin

sequence_source: UniProtKB A0A140H631 direct lookup; active TrEMBL entry, sequence version 1, retrieved 2026-06-06

enzyme: glucan endo-1,3-beta-D-glucosidase

substrate: Laminarin


organism: Bacillus tequilensis

substrate_name: Barley beta-glucan

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

substrate: Barley beta-glucan


organism: Cellulosimicrobium cellulans

sequence_source: UniProtKB O68641 direct lookup; active TrEMBL entry, sequence version 1, retrieved 2026-06-06


proof_lines: mutant enzyme T149A/G145D/A344V, at 37°C


organism: Formosa agariphila

sequence_source: UniProtKB T2KMB6 direct lookup; active TrEMBL entry, sequence version 1, retrieved 2026-06-06

proof_lines: substrate source Saccharina cichorioides, pH 5.5, 37°C


organism: Caenorhabditis elegans


organism: Arabidopsis thaliana

proof_lines: pH and temperature not specified in the publication


organism: Ascaris suum

proof_lines: pH 7.8, 22°C, recombinant His-tagged enzyme


proof_lines: 30°C, pH 8, varied substrate: ethanolamine phosphate

proof_lines: 30°C, pH 8, varied substrate: S-adenosyl-L-methionine


organism: Cavia porcellus

substrate_name: sn-glycerol 3-phosphate

substrate: sn-glycerol 3-phosphate


organism: Cucurbita moschata

substrate_name: acyl-ACP

mutation_signature: recombinant N-terminal truncated acyltransferase recombinant N-terminal truncated acyltransferase

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

substrate: acyl-ACP


substrate_name: glycerol 3-phosphate

proof_lines: L261F mutant acyltransferase, acyl-donor oleoyl-CoA

proof_lines: L261F mutant acyltransferase, acyl-donor palmitoyl-CoA

substrate: glycerol 3-phosphate


substrate_name: oleoyl-CoA

proof_lines:
recombinant stromal acyltransferase
acyl donor palmitoyl-CoA
acyl donor oleoyl-CoA

substrate: oleoyl-CoA


organism: Escherichia coli

proof_lines: strain VL3/pVL1 bearing plasmid which overproduces glycerol 3-phosphate acyltransferase, reconstituted enzyme

proof_lines: acyl donor palmitoyl-CoA or palmitoyl-ACP


organism: Euglena sp.

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


organism: Helianthus annuus

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA


organism: Lathyrus oleraceus


organism: Leishmania major

proof_lines: pH 7.5, 26°C, recombinant enzyme in cell extracts of enzyme-deficient yeast mutant cells strain BYL118


sequence_source: UniProtKB:E9ACF5 canonical sequence via UniProt REST; UniProt GO activity/process cross-references PMID 15819633.

proof_lines: pH 7.5, 26°C, wild-type enzyme in cell extracts of promastigote


organism: Macrobrachium borellii

proof_lines: Vmax value calculated with oleoyl-CoA as a substrate is 4fold lower than the value obtained with palmitoyl-CoA


organism: Mus musculus

sequence_source: UniProtKB:Q14DK4 canonical sequence via UniProt REST; PubMed PMID 14724270 is attached to UniProt GO activity/localization evidence for GPAT2.


organism: Oryctolagus cuniculus


organism: Persea americana


organism: Rattus norvegicus

substrate_name: mixed acyl-CoA and glycerol-3-phosphate source group

proof_lines: mitochondrial acyl transferase reconstituted in asolectin

proof_lines: mitochondrial acyl transferase reconstituted in 1,2-dioleoylphosphatidylglycerol

proof_lines: mitochondrial acyl transferase reconstituted in 1,2-dipalmitoylphosphatidylglycerol


organism: Saccharomyces cerevisiae


organism: Schistocerca gregaria


organism: Spinacia oleracea

proof_lines: acyl donors: palmitoyl-ACP or stearoyl-ACP


organism: Theobroma cacao

substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


organism: Umbelopsis ramanniana


organism: Acetivibrio thermocellus

substrate_name: cyclic 2',3'-AMP

substrate: cyclic 2',3'-AMP


organism: Cucumis melo


organism: Cryptopygus antarcticus

substrate_name: 1% laminarin (at pH 6.0 and 50 degrees Celsius)

assay_conditions_summary: pH 6


organism: Thermobifida fusca (strain YX)

substrate_name: laminarin (at 28 degrees Celsius and pH 6.8)


organism: Hordeum vulgare

sequence_source: UniProtKB:P15737 direct REST lookup 2026-06-06


substrate_name: H2O; Laminarin

sequence_source: UniProtKB:P34742 direct REST lookup 2026-06-06

substrate: H2O; Laminarin


organism: Lentinula edodes

sequence_source: UniProtKB:G9M5R4 direct REST lookup 2026-06-06


organism: Oryza sativa

sequence_source: UniProtKB:Q9ZNY9 direct REST lookup 2026-06-06


organism: Pyrococcus furiosus

sequence_variant_note: Resolved canonical sequence from UniProtKB:O73951 direct REST lookup 2026-06-06 and applied mutation signature S296C to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 90°C, S296C variant immobilized on beads of 0.063-0.09 mM size

proof_lines: pH 6.5, 90°C, S296C variant immobilized on beads of 0.02-0.04 mM size


organism: Shouchella lehensis

sequence_source: UniProtKB:A0A0K0KAZ7 direct REST lookup 2026-06-06

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


organism: Spodoptera frugiperda

sequence_source: UniProtKB:A6YQV6 direct REST lookup 2026-06-06


organism: Tenebrio molitor

sequence_source: UniProtKB:C6GFH7 direct REST lookup 2026-06-06


organism: Arabidopsis thaliana

substrate_name: D-glucuronic acid 1-phosphate

sequence_source: UniProtKB:Q9C5I1 direct lookup

substrate: D-glucuronic acid 1-phosphate


substrate_name: UDPgalactose; Diphosphate

sequence_source: UniProtKB:Q0GZS3 direct lookup

substrate: UDPgalactose; Diphosphate


organism: Giardia duodenalis

substrate_name: D-galactose 1-phosphate

proof_lines: cosubstrate UTP, S0.5 value, pH 8.0, 37°C

proof_lines: cosubstrate D-glucose 1-phosphate, S0.5 value, pH 8.0, 37°C

proof_lines: cosubstrate D-galactose 1-phosphate, S0.5 value, pH 8.0, 37°C

substrate: D-galactose 1-phosphate


organism: Glycine max

sequence_source: UniProtKB:Q09WE7 direct lookup

proof_lines: pH 8.0, cosubstrate: glucose 1-phosphate

proof_lines: pH 8.0, cosubstrate: glucuronic acid 1-phosphate


organism: Hordeum vulgare subsp. vulgare

substrate_name: alpha-D-galactose 1-phosphate

sequence_source: UniProtKB:F2DQG9 direct lookup

substrate: alpha-D-galactose 1-phosphate


organism: Lathyrus oleraceus

substrate_name: diphosphate

sequence_source: UniProtKB:Q5W915 direct lookup

proof_lines:
pH 7.0, 35°C
D-glucose 1-phosphate, pH 7.0, 35°C

substrate: diphosphate


organism: Leishmania major

sequence_source: UniProtKB:D3G6S4 direct lookup; PMID 19906649 paper-linked accession in the source bundle


substrate_name: UDP-L-arabinopyranose

column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section B (reverse reaction); varied-substrate row 'UDP-L-Arap'; column 'Km (uM)' = 373; column 'Vmax (umol/min/mg)' = 63; column 'kcat (s^-1)' = 72; column 'Efficiency kcat/Km (M^-1 s^-1)' = 1.98 x 10^5; column 'Efficiency %' = 9.

normalized_value_unit_evidence: Km: printed Table 2 cell 373 uM; 373 / 1000 = 0.373 mM. kcat: printed Table 2 cell 72 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 72.0 s^(-1). kcat/Km: printed Table 2 cell 1.98 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.98 x 10^5 / 1000 = 198.0 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section B (reverse reaction), varied-substrate row 'UDP-L-Arap': Km = 373 uM; kcat = 72 s^-1; printed kcat/Km = 1.98 x 10^5 M^-1 s^-1.

substrate: UDP-L-arabinopyranose


organism: Trypanosoma cruzi

substrate_name: D-xylose 1-phosphate

sequence_source: UniProtKB accession D3YBH2 direct lookup

substrate: D-xylose 1-phosphate


substrate_name: UDP-D-glucose

substrate: UDP-D-glucose


organism: Formosa algae

substrate_name: Laminarin

sequence_source: UniProtKB accession A0A0B5GQL6 direct lookup

proof_lines: substrate source Saccharina cichorioides, pH 5.5, 37°C

substrate: Laminarin


sequence_source: UniProtKB accession Q02126 direct lookup


sequence_source: UniProtKB accession P34742 direct lookup


substrate_name: Laminarin; H2O

sequence_source: UniProtKB accession P15737 direct lookup

substrate: Laminarin; H2O


substrate_name: glucuronic acid-1-phosphate

proof_lines: High activity with glucose-1-phosphate > glucuronic acid-1-phosphate > galactose-1-phosphate, but low or no activity with N-acetylglucosamine-1-phosphate, fucose-1-phosphate, mannose-1-phosphate, inositol-1-phosphate or glucose-6-phosphate.

substrate: glucuronic acid-1-phosphate


proof_lines: High activity with galactose-1-phosphate, glucose-1-phosphate or glucuronic acid-1-phosphate, but low or no activity with N-acetylglucosamine-1-phosphate, mannose-1-phosphate or glucose-6-phosphate.


organism: Pisum sativum

substrate_name: UTP

proof_lines: High activity with galactose-1-phosphate > glucose-1-phosphate > glucuronic acid-1-phosphate, but low or no activity with N-acetylglucosamine-1-phosphate, fucose-1-phosphate, mannose-1-phosphate or glucose-6-phosphate.

substrate: UTP


organism: Acetivibrio thermocellus


organism: Bacillus subtilis

substrate_name: bis-p-nitrophenyl phosphate

substrate: bis-p-nitrophenyl phosphate


organism: Bos taurus

sequence_source: UniProtKB:P06623 reviewed Swiss-Prot CN37_BOVIN, Bos taurus CNP/CNPase, EC 3.1.4.37

proof_lines:
bovine brain
bovine spinal cord
bovine brain, elastase fragment


organism: Danio rerio


substrate_name: D-glucose 1-phosphate

column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section A (forward reaction); varied-substrate row 'Glc-1-P'; column 'Km (uM)' = 1706; column 'Vmax (umol/min/mg)' = 166; column 'kcat (s^-1)' = 191; column 'Efficiency kcat/Km (M^-1 s^-1)' = 1.14 x 10^5; column 'Efficiency %' = 5.

normalized_value_unit_evidence: Km: printed Table 2 cell 1706 uM; 1706 / 1000 = 1.706 mM. kcat: printed Table 2 cell 191 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 191.0 s^(-1). kcat/Km: printed Table 2 cell 1.14 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.14 x 10^5 / 1000 = 114.0 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section A (forward reaction), varied-substrate row 'Glc-1-P': Km = 1706 uM; kcat = 191 s^-1; printed kcat/Km = 1.14 x 10^5 M^-1 s^-1.

substrate: D-glucose 1-phosphate


column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section A (forward reaction); varied-substrate row 'Gal-1-P'; column 'Km (uM)' = 860; column 'Vmax (umol/min/mg)' = 190; column 'kcat (s^-1)' = 219; column 'Efficiency kcat/Km (M^-1 s^-1)' = 2.59 x 10^5; column 'Efficiency %' = 12.

normalized_value_unit_evidence: Km: printed Table 2 cell 860 uM; 860 / 1000 = 0.86 mM. kcat: printed Table 2 cell 219 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 219.0 s^(-1). kcat/Km: printed Table 2 cell 2.59 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.59 x 10^5 / 1000 = 259.0 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section A (forward reaction), varied-substrate row 'Gal-1-P': Km = 860 uM; kcat = 219 s^-1; printed kcat/Km = 2.59 x 10^5 M^-1 s^-1.


source_db: brenda/skid

proof_lines: reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25°C

proof_lines: reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25°C

proof_lines: reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25°C

source: brenda/skid


substrate_name: UDP-D-galactose

column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section B (reverse reaction); varied-substrate row 'UDP-Gal'; column 'Km (uM)' = 148; column 'Vmax (umol/min/mg)' = 134; column 'kcat (s^-1)' = 154; column 'Efficiency kcat/Km (M^-1 s^-1)' = 1.07 x 10^6; column 'Efficiency %' = 51.

normalized_value_unit_evidence: Km: printed Table 2 cell 148 uM; 148 / 1000 = 0.148 mM. kcat: printed Table 2 cell 154 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 154.0 s^(-1). kcat/Km: printed Table 2 cell 1.07 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.07 x 10^6 / 1000 = 1070.0 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section B (reverse reaction), varied-substrate row 'UDP-Gal': Km = 148 uM; kcat = 154 s^-1; printed kcat/Km = 1.07 x 10^6 M^-1 s^-1.

substrate: UDP-D-galactose


substrate_name: UDP-alpha-D-galacturonate

proof_lines: reverse reaction, UDP-beta-L-arabinopyranose, pH 7.8, 25°C

proof_lines: reverse reaction, UDP-alpha-D-galacturonate, pH 7.8, 25°C

substrate: UDP-alpha-D-galacturonate


column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section A (forward reaction); varied-substrate row 'UTP (Glc-1-P)'; column 'Km (uM)' = 116; column 'Vmax (umol/min/mg)' = 181; column 'kcat (s^-1)' = 209; column 'Efficiency kcat/Km (M^-1 s^-1)' = 1.83 x 10^6; column 'Efficiency %' = 88.

normalized_value_unit_evidence: Km: printed Table 2 cell 116 uM; 116 / 1000 = 0.116 mM. kcat: printed Table 2 cell 209 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 209.0 s^(-1). kcat/Km: printed Table 2 cell 1.83 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.83 x 10^6 / 1000 = 1830.0 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section A (forward reaction), varied-substrate row 'UTP (Glc-1-P)': Km = 116 uM; kcat = 209 s^-1; printed kcat/Km = 1.83 x 10^6 M^-1 s^-1.


column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section B (reverse reaction); varied-substrate row 'UDP-Glc'; column 'Km (uM)' = 174; column 'Vmax (umol/min/mg)' = 157; column 'kcat (s^-1)' = 180; column 'Efficiency kcat/Km (M^-1 s^-1)' = 1.06 x 10^6; column 'Efficiency %' = 51.

normalized_value_unit_evidence: Km: printed Table 2 cell 174 uM; 174 / 1000 = 0.174 mM. kcat: printed Table 2 cell 180 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 180.0 s^(-1). kcat/Km: printed Table 2 cell 1.06 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.06 x 10^6 / 1000 = 1060.0 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section B (reverse reaction), varied-substrate row 'UDP-Glc': Km = 174 uM; kcat = 180 s^-1; printed kcat/Km = 1.06 x 10^6 M^-1 s^-1.


substrate_name: UDP-D-galacturonate

column_label: Table 2: L. major UDP-sugar pyrophosphorylase kinetic parameters (J. Biol. Chem. 2010, 285(2):878-887); section B (reverse reaction); varied-substrate row 'UDP-GalA'; column 'Km (uM)' = 790; column 'Vmax (umol/min/mg)' = 11; column 'kcat (s^-1)' = 13; column 'Efficiency kcat/Km (M^-1 s^-1)' = 1.67 x 10^4; column 'Efficiency %' = 1.

normalized_value_unit_evidence: Km: printed Table 2 cell 790 uM; 790 / 1000 = 0.79 mM. kcat: printed Table 2 cell 13 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies and the value stays 13.0 s^(-1). kcat/Km: printed Table 2 cell 1.67 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.67 x 10^4 / 1000 = 16.7 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value carried forward for kcat_over_km.

raw_value_unit_evidence: Table 2, section B (reverse reaction), varied-substrate row 'UDP-GalA': Km = 790 uM; kcat = 13 s^-1; printed kcat/Km = 1.67 x 10^4 M^-1 s^-1.

substrate: UDP-D-galacturonate


organism: Escherichia coli

substrate_name: cyclic 2',3'-GMP

proof_lines:
pH 7, 37°C
hydrolysis of cyclic 2,3-AMP

substrate: cyclic 2',3'-GMP


organism: Homo sapiens


organism: Mus musculus


organism: Rattus norvegicus


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4QE75 direct lookup; V330W/F383R sequence reconstructed from PMID 30871023 Table 4 when mutant. and applied mutation signature V330W/F383R to reconstruct the assayed variant sequence.

proof_lines: mutant V330W/F383R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4QE75 direct lookup; V330W sequence reconstructed from PMID 30871023 Table 4 when mutant. and applied mutation signature V330W to reconstruct the assayed variant sequence.

proof_lines: mutant V330W, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4QE75 direct lookup; V199W sequence reconstructed from PMID 30871023 Table 4 when mutant. and applied mutation signature V199W to reconstruct the assayed variant sequence.

proof_lines: mutant F199W, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q4QE75 direct lookup; F383R sequence reconstructed from PMID 30871023 Table 4 when mutant. and applied mutation signature F383R to reconstruct the assayed variant sequence.

proof_lines: mutant F383Rd-type enzyme, pH and temperature not specified in the publication


sequence_source: UniProtKB Q4QE75 direct lookup; Wild type sequence reconstructed from PMID 30871023 Table 4 when mutant.

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


substrate_name: UTP; D-Glucose 1-phosphate

sequence_source: UniProtKB Q5W915 direct lookup

substrate: UTP; D-Glucose 1-phosphate


substrate_name: TTP

sequence_source: UniProtKB D3YBH2 direct lookup

substrate: TTP


organism: Thermotoga petrophila

km_unit: mg/mL

sequence_source: UniProtKB:A5IL44 direct accession check, 2026-06-06


organism: Vitis vinifera


sequence_source: UniProtKB:A7PQW3 direct accession check, 2026-06-06


sequence_source: UniProtKB:Q9M563 direct accession check, 2026-06-06


sequence_source: UniProtKB:F6HLL8 direct accession check, 2026-06-06


enzyme_display_name: biphenyl-2,3-diol 1,2-dioxygenase

organism: Achromobacter sp.

enzyme: biphenyl-2,3-diol 1,2-dioxygenase


substrate_name: catechol

substrate: catechol


organism: Burkholderia xenovorans LB400

substrate_name: Biphenyl-2,3-diol; O2

sequence_source: UniProtKB:P47228 direct lookup; reviewed Swiss-Prot entry BPHC_PARXL; sequence version 2; entry version 163; accessed 2026-06-06

substrate: Biphenyl-2,3-diol; O2


organism: Arabidopsis thaliana

substrate_name: dTTP

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

substrate: dTTP


organism: Lathyrus oleraceus

substrate_name: D-galacturonic acid 1-phosphate

substrate: D-galacturonic acid 1-phosphate


organism: Populus deltoides


organism: Thermus caldophilus

substrate_name: N-acetylglucosamine 1-phosphate

substrate: N-acetylglucosamine 1-phosphate


organism: Trypanosoma cruzi

substrate_name: D-xylose 1-phosphate

proof_lines: co-substrate: glucose 1-phosphate, pH 7.6, 37°C

substrate: D-xylose 1-phosphate


organism: Acetivibrio thermocellus

substrate_name: cyclic 2',3'-AMP

sequence_variant_note: Resolved canonical sequence from UniProtKB:A3DJ38 canonical sequence with direct R237Q reconstruction; PubMed/PMCID table row names mutant R237Q and applied mutation signature R237Q to reconstruct the assayed variant sequence.

substrate: cyclic 2',3'-AMP


organism: Delftia acidovorans

proof_lines: pH 9.0, 25°C, recombinant His-tagged enzyme


organism: Dyella ginsengisoli


organism: Pseudomonas putida


organism: Burkholderia cepacia

proof_lines:
reversible substrate inhibition
3-methylcatechol as substrate
catechol as substrate


organism: Comamonas testosteroni

proof_lines:
3,3-dichlorobiphenyl as substrate
biphenyl as substrate
2,2-dichlorobiphenyl as substrate


proof_lines:
pH 8.0, 30°C, free enzyme
pH 8.0, 30°C, immobilized enzyme


organism: Ectopseudomonas oleovorans


organism: Metapseudomonas resinovorans


enzyme_display_name: meprin A

organism: Mus musculus

substrate_name: Phe5(4-nitro)bradykinin; H2O

sequence_source: UniProtKB reviewed P28825 (MEP1A_MOUSE), direct REST lookup; sequence version 4, length 747.

enzyme: meprin A

substrate: Phe5(4-nitro)bradykinin; H2O


organism: Homo sapiens

substrate_name: GRP

substrate: GRP


organism: Rhodococcus pyridinivorans

sequence_source: UniProtKB Q6QF56 direct REST/FASTA lookup; TrEMBL entry Q6QF56_9NOCA, gene bphC2


sequence_source: UniProtKB Q6QF57 direct REST/FASTA lookup; TrEMBL entry Q6QF57_9NOCA, gene bphC1, entry flagged Fragment


organism: uncultured bacterium

sequence_source: NCBI GenBank HQ334892.1 CDS translation, protein_id AEA36111.1; UniProtKB F2X5L9 direct lookup reports DELETED


organism: Pseudomonas sp.


organism: Pseudomonas sp. HA10


organism: Rhodococcus globerulus


organism: Sphingomonas sp.


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


proof_lines: mutant enzyme E79H, at pH 7.5, temperature not specified in the publication


organism: Paraburkholderia xenovorans (strain LB400)

proof_lines: Substrate inhibition occurs at 300 uM (+/- 20 uM).


organism: Sus scrofa

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


substrate_name: P1,P4-Bis(5'-adenosyl) tetraphosphate

sequence_source: UniProtKB:P50583 direct accession check

substrate: P1,P4-Bis(5'-adenosyl) tetraphosphate


substrate_name: Unknown

substrate: Unknown


organism: Lupinus angustifolius

sequence_source: UniProtKB:O04841 direct accession check

proof_lines: Ki about 0.005 mM, in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% (v/v) DMSO, at 25°C

proof_lines: in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% DMSO, at 25°C


organism: Myxococcus xanthus


organism: Plasmodium falciparum

substrate_name: 5',5''-diadenosine tetraphosphate

sequence_source: UniProtKB:C0H4F3 direct accession check

substrate: 5',5''-diadenosine tetraphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:C0H4F3 direct accession check plus explicit P133A reconstruction and applied mutation signature P133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C0H4F3 FASTA plus row-specific P133F reconstruction and applied mutation signature P133F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C0H4F3 FASTA


sequence_source: UniProtKB:Q16819 canonical sequence, reviewed Swiss-Prot entry MEP1A_HUMAN, retrieved via rest.uniprot.org on 2026-06-06.

proof_lines: pH and temperature not specified in the publication


organism: Aquifex aeolicus

substrate_name: P1,P6-bis(5'-adenosyl) hexaphosphate

sequence_source: UniProtKB:O66548 canonical sequence, unreviewed TrEMBL entry O66548_AQUAE, retrieved via rest.uniprot.org on 2026-06-06.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines: in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C

substrate: P1,P6-bis(5'-adenosyl) hexaphosphate


substrate_name: P1,P4-bis(5'-adenosyl) tetraphosphate

substrate: P1,P4-bis(5'-adenosyl) tetraphosphate


substrate_name: P1,P5-bis(5'-adenosyl) pentaphosphate

substrate: P1,P5-bis(5'-adenosyl) pentaphosphate


organism: Caenorhabditis elegans

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

sequence_source: UniProtKB:Q9U2M7 canonical sequence, reviewed Swiss-Prot entry AP4A_CAEEL, retrieved via rest.uniprot.org on 2026-06-06.

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C

proof_lines: in 5 0mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C

source_databases_merged: sabio_rk brenda skid


organism: Rattus norvegicus


proof_lines: pH 6, 25°C, recombinant full-length wild-type CNP1


substrate_name: dATP

sequence_source: UniProtKB Q9U2M7 direct REST lookup on 2026-06-06

substrate: dATP


substrate_name: dGTP

substrate: dGTP


organism: Deinococcus radiodurans

sequence_source: UniProtKB Q9RRX6 direct REST lookup on 2026-06-06


assay_conditions_summary: cofactor ATP


organism: Drosophila melanogaster

substrate_name: 5',5'-diadenosine hexaphosphate

sequence_source: UniProtKB Q4V6M1 direct REST lookup on 2026-06-06

substrate: 5',5'-diadenosine hexaphosphate


organism: Homo sapiens

sequence_source: UniProtKB P50583 direct REST lookup on 2026-06-06


proof_lines: pH 6, 25°C, catalytic fragment of CNP1 corresponding to the C-terminal 250 amino acids


organism: Triticum aestivum

substrate_name: H2O; 2',3'-Cyclic AMP

substrate: H2O; 2',3'-Cyclic AMP


substrate_name: maltopentose

proof_lines: IP-SI, immunoprecipitated human sucrase-isomaltase complex

proof_lines: versus the C-terminal subunit, pH and temperature not specified in the publication

proof_lines: versus the N-terminal subunit, pH and temperature not specified in the publication

substrate: maltopentose


organism: Parageobacillus thermoglucosidasius

substrate_name: isomaltose

substrate: isomaltose


organism: Saccharomyces cerevisiae

substrate_name: 4-nitrophenyl alpha-D-glucopyranoside

substrate: 4-nitrophenyl alpha-D-glucopyranoside


organism: Suncus murinus


substrate_name: maltose

substrate: maltose


organism: Thermoanaerobium sp.

substrate_name: p-nitrophenyl-alpha-D-glucopyranoside

substrate: p-nitrophenyl-alpha-D-glucopyranoside


organism: Zalophus californianus

assay_conditions_summary: pH 6.8; buffer 33 mM sodium maleate


enzyme_display_name: beta-mannosidase

organism: Aplysia fasciata

substrate_name: p-nitrophenyl-beta-D-mannoside

enzyme: beta-mannosidase

substrate: p-nitrophenyl-beta-D-mannoside


organism: Aspergillus niger


organism: Bacillus sp. (in: firmicutes)

substrate_name: p-nitrophenyl-beta-D-mannopyranoside

substrate: p-nitrophenyl-beta-D-mannopyranoside


organism: Bacteroides thetaiotaomicron

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8AAK6 canonical sequence; E555A reconstructed after direct residue check; RCSB 2JE8 and PMID 17287210 anchor BtMan2A. and applied mutation signature E555A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E555A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8AAK6 canonical sequence; W395A reconstructed after direct residue check; RCSB 2JE8 and PMID 17287210 anchor BtMan2A. and applied mutation signature W395A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W395A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


organism: Bacillus cereus


substrate_name: phenyl-alpha-D-glucopyranoside

substrate: phenyl-alpha-D-glucopyranoside


organism: Bacillus sp. F5

substrate_name: isomaltotriose

substrate: isomaltotriose


substrate_name: trehalose

substrate: trehalose


organism: Exiguobacterium artemiae


proof_lines: mutant enzyme A109P/S130P, at pH 7.0 and 25°C


proof_lines: mutant enzyme A109P/S130P/E176P/K441P, at pH 7.0 and 25°C


organism: Heyndrickxia coagulans

substrate_name: p-nitrophenyl alpha-D-glucopyranoside

substrate: p-nitrophenyl alpha-D-glucopyranoside


organism: Anoxybacillus gonensis

substrate_name: sucrose

proof_lines:
pH 7.0, 60°C
at pH 7.0 and 60°C

substrate: sucrose


organism: Arthrobacter globiformis


proof_lines: recombinant wild-type enzyme, pH 7.0, 35°C


organism: Bacillus subtilis


proof_lines: mutant enzyme A109P/S130P/E176P, at pH 7.0 and 25°C


enzyme_display_name: bacterial sulfide:quinone reductase

organism: Acidithiobacillus ferrooxidans

substrate_name: decylubiquinone; Sulfide

sequence_source: UniProtKB reviewed entry B7JBP8 FASTA

proof_lines: in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication

enzyme: bacterial sulfide:quinone reductase

substrate: decylubiquinone; Sulfide


substrate_name: Sulfide

sequence_variant_note: Resolved canonical sequence from UniProtKB B7JBP8 canonical sequence with selected-row mutation signature applied and applied mutation signature H132A to reconstruct the assayed variant sequence.

smiles: S

substrate: Sulfide


sequence_variant_note: Resolved canonical sequence from UniProtKB B7JBP8 canonical sequence with selected-row mutation signature applied and applied mutation signature C356S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB B7JBP8 canonical sequence with selected-row mutation signature applied and applied mutation signature C128S to reconstruct the assayed variant sequence.


substrate_name: Sulfide; decylubiquinone

sequence_source: UniProtKB B7JBP8 canonical sequence with selected-row mutation signature applied

substrate: Sulfide; decylubiquinone


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


sequence_variant_note: Resolved canonical sequence from UniProtKB B7JBP8 canonical sequence with selected-row mutation signature applied and applied mutation signature C160S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB B7JBP8 canonical sequence with selected-row mutation signature applied and applied mutation signature C128A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for B7JBP8 on 2026-06-06 and applied mutation signature H132A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct accession lookup for B7JBP8 on 2026-06-06

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 REST direct accession lookup for B7JBP8 on 2026-06-06 and applied mutation signature C128A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for B7JBP8 on 2026-06-06 and applied mutation signature C160A to reconstruct the assayed variant sequence.


organism: Aphanothece halophytica

sequence_source: UniProtKB REST direct accession lookup for Q9KI50 on 2026-06-06

proof_lines: in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication


organism: Aquifex aeolicus

sequence_source: UniProtKB REST direct accession lookup for O67931 on 2026-06-06

proof_lines:
in 50 mM Tris-HCl, pH 7.4, 40°C
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=40°C, pH=7.4


organism: Chlorobaculum tepidum

sequence_source: UniProtKB REST direct accession lookup for Q8KDG3 on 2026-06-06


enzyme_display_name: choloylglycine hydrolase

organism: Enterococcus faecalis

substrate_name: taurodeoxycholic acid

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

proof_lines:
about, pH 5.0, 50°C, recombinant enzyme
pH 5.0, 50°C, recombinant enzyme
Raw SKiD Env: Temp=50°C, pH=5

enzyme: choloylglycine hydrolase

substrate: taurodeoxycholic acid


substrate_name: taurochenodeoxycholic acid

substrate: taurochenodeoxycholic acid


substrate_name: glycocholic acid

substrate: glycocholic acid


organism: Lactiplantibacillus plantarum

substrate_name: Leu-cholic acid

substrate: Leu-cholic acid


organism: Lactobacillus johnsonii

substrate_name: Taurocholate; H2O

substrate: Taurocholate; H2O


substrate_name: H2O; Taurocholate

substrate: H2O; Taurocholate


organism: Ligilactobacillus salivarius

assay_conditions_summary: pH 5.4; 310.15 K; buffer the pH 6.0 reaction

column_label: Table 1 (Activity and kinetics of rBSH for different bile salts), substrate row 'TCDCA'; column 'BSH activity (umol/min/mg)' = 8.0 +/- 2.37; column 'Relative activity (%)' = 45.1; column 'Km (mM)' = 2.53; column 'kcat (min^-1)' = 510; column 'kcat/Km (min^-1 mM^-1)' = 201.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.53 mM; the printed unit is already mM, so no unit conversion applies and the paper value is 2.53 mM, while the export carries 2.75 mM. kcat: printed Table 1 cell 510 min^-1; 510 / 60 = 8.5 s^-1, which is the exported kcat 8.5 s^(-1). kcat/Km: printed Table 1 cell 201 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 201 / 60 = 3.35 s^-1 mM^-1, and the export carries 3.090909090909091 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row 'TCDCA' (taurochenodeoxycholic acid): Km = 2.53 mM; kcat = 510 min^-1; printed kcat/Km = 201 min^-1 mM^-1.

table_label: Table 1: Activity and kinetics of rBSH for different bile salts (Applied and Environmental Microbiology 2012, 78(24):8795-8802)


organism: Thiocapsa roseopersicina

substrate_name: duroquinone

sequence_source: UniProt A0A1Z2RRG1 FASTA direct lookup on 2026-06-06; entry header OS=Thiocapsa roseopersicina, GN=sqrF.

substrate: duroquinone


sequence_variant_note: Resolved canonical sequence from UniProt A0A1Z2RRG1 FASTA direct lookup on 2026-06-06; C272A variant reconstructed by applying the selected mutation signature to that canonical sequence. and applied mutation signature C272A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt A0A1Z2RRG1 FASTA direct lookup on 2026-06-06; C332A variant reconstructed by applying the selected mutation signature to that canonical sequence. and applied mutation signature C332A to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 8.0, 25°C


sequence_source: UniProt A0A1Z2RRG1 FASTA direct lookup on 2026-06-06; C272A variant reconstructed by applying the selected mutation signature to that canonical sequence.


sequence_source: UniProt A0A1Z2RRG1 FASTA direct lookup on 2026-06-06; C332A variant reconstructed by applying the selected mutation signature to that canonical sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_manual_substitution and applied mutation signature C49A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_manual_substitution and applied mutation signature C272A to reconstruct the assayed variant sequence.


organism: Clostridium perfringens

substrate_name: H2O; Glycocholate

substrate: H2O; Glycocholate


substrate_name: glycochenodeoxycholic acid

substrate: glycochenodeoxycholic acid


substrate_name: glycodeoxycholic acid

substrate: glycodeoxycholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


organism: Bifidobacterium longum

substrate_name: glycocholate (at 37 degrees Celsius and pH 5.5)

sequence_source: source_record; direct UniProt Q9KK62 FASTA check

proof_lines: kcat is 85 sec(-1) with glycocholate as substrate. kcat is 76 sec(-1) with taurocholate as substrate (at 40 degrees Celsius and pH 6.5).


proof_lines: pH 6.5, 37°C, recombinant isozyme BSH2, in presence of DTT

proof_lines: pH 6.5, 37°C, recombinant isozyme BSH1, in presence of DTT


organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)

substrate_name: sodium sulfide

substrate: sodium sulfide


organism: Clostridium perfringens (strain 13 / Type A)

substrate_name: taurocholate (in the TCA deconjugation assay)


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

substrate_name: glycodeoxycholate

substrate: glycodeoxycholate


organism: Homo sapiens

substrate_name: cyanide

sequence_source: UniProtKB Q9Y6N5 direct REST lookup on 2026-06-06

smiles: C#N

substrate: cyanide


substrate_name: coenzyme Q

substrate: coenzyme Q


substrate_name: Sulfide

substrate: Sulfide


proof_lines: cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C

proof_lines: with coenzyme Q as cosubstrate, at pH 8.0 and 25°C


organism: Rhodobacter capsulatus

sequence_source: UniProtKB Q52722 direct REST lookup on 2026-06-06

proof_lines: in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication


organism: Thiobacillus ferrooxidans

substrate_name: n n Sulfide; n n Decylubiquinone

sequence_source: UniProtKB B7JBP8 direct REST lookup on 2026-06-06

substrate: n n Sulfide; n n Decylubiquinone


sequence_source: UniProtKB J7H3P9 direct REST lookup on 2026-06-06

column_label: Table 1 (Activity and kinetics of rBSH for different bile salts), substrate row 'GCDCA'; column 'BSH activity (umol/min/mg)' = 17.7 +/- 1.18; column 'Relative activity (%)' = 100; column 'Km (mM)' = 2.48; column 'kcat (min^-1)' = 938; column 'kcat/Km (min^-1 mM^-1)' = 378.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.48 mM; the printed unit is already mM, so no unit conversion applies and the paper value is 2.48 mM, while the export carries 1.15 mM. kcat: printed Table 1 cell 938 min^-1; 938 / 60 = 15.633333333333333 s^-1, which this catalog row and the 29 source records behind it carry at three significant figures as 15.6 s^(-1); this record keeps that metric as carried and proposes no change to it. kcat/Km: printed Table 1 cell 378 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 378 / 60 = 6.3 s^-1 mM^-1, and this catalog row carries no exported efficiency value.

raw_value_unit_evidence: Table 1, substrate row 'GCDCA' (glycochenodeoxycholic acid): Km = 2.48 mM; kcat = 938 min^-1; printed kcat/Km = 378 min^-1 mM^-1.


sequence_source: UniProtKB REST direct lookup for Q9Y6N5


substrate_name: sulfite

substrate: sulfite


substrate_name: glycocholic acid

sequence_source: UniProtKB J7H3P9 REST FASTA and JSON checked 2026-06-06; entry references PMID 23064348 and EMBL JX120368.


column_label: Table 1 (Activity and kinetics of rBSH for different bile salts), substrate row 'TCA'; column 'BSH activity (umol/min/mg)' = 5.6 +/- 0.33; column 'Relative activity (%)' = 31.4; column 'Km (mM)' = 3.21; column 'kcat (min^-1)' = 585; column 'kcat/Km (min^-1 mM^-1)' = 182.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.21 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 3.21 mM. kcat: printed Table 1 cell 585 min^-1; 585 / 60 = 9.75 s^-1, and the exported value is 9.75 s^(-1). kcat/Km: the exported 3.0373831775700935 s^(-1)*mM^(-1) is the full-precision quotient 9.75 / 3.21 of the two printed component cells; the paper's own printed efficiency cell 182 min^-1 mM^-1 converts as 182 / 60 = 3.033333333333333 s^-1 mM^-1, which is that quotient (9.75 / 3.21 = 182.2429906542056 min^-1 mM^-1) rounded to the whole-number precision the table prints.

raw_value_unit_evidence: Table 1, substrate row 'TCA' (taurocholic acid): Km = 3.21 mM; kcat = 585 min^-1; printed kcat/Km = 182 min^-1 mM^-1.


substrate_name: taurodeoxycholic acid

substrate: taurodeoxycholic acid


organism: Bacteroides thetaiotaomicron

substrate_name: p-nitrophenyl-beta-D-mannopyranoside

sequence_variant_note: Resolved canonical sequence from UniProt Q8AAK6 canonical sequence with direct W200A substitution after confirming residue 200 is W; paper-linked RCSB 2JE8 anchors Q8AAK6 to BtMan2A. and applied mutation signature W200A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W200A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin

substrate: p-nitrophenyl-beta-D-mannopyranoside


sequence_variant_note: Resolved canonical sequence from UniProt Q8AAK6 canonical sequence with direct D199A substitution after confirming residue 199 is D; paper-linked RCSB 2JE8 anchors Q8AAK6 to BtMan2A. and applied mutation signature D199A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D199A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from UniProt Q8AAK6 canonical sequence with direct E462A substitution after confirming residue 462 is E; paper-linked RCSB 2JE8 anchors Q8AAK6 to BtMan2A. and applied mutation signature E462A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E462A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from UniProt Q8AAK6 canonical sequence with direct N461A substitution after confirming residue 461 is N; paper-linked RCSB 2JE8 anchors Q8AAK6 to BtMan2A. and applied mutation signature N461A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N461A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from UniProt Q8AAK6 canonical sequence with direct Y537A substitution after confirming residue 537 is Y; paper-linked RCSB 2JE8 anchors Q8AAK6 to BtMan2A. and applied mutation signature Y537A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y537A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


organism: Capra hircus

substrate_name: 4-methylumbelliferyl beta-D-mannopyranoside; p-nitrophenyl-beta-D-mannoside; p-nitrophenyl beta-D-mannopyranoside

proof_lines:
lysosomal, acidic enzyme
nonlysosomal, neutral enzyme


organism: Cellulomonas fimi

substrate_name: Unknown

substrate: Unknown


organism: Cellvibrio mixtus

substrate_name: 4-nitrophenyl-beta-D-mannopyranose; 4-O-beta-D-mannopyranosyl-D-mannopyranose; beta-D-mannosyl-1,4-beta-D-glucoside; Mannotriose; mannobiose


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


organism: Ceratonia siliqua

substrate_name: p-nitrophenyl-beta-D-mannoside

substrate: p-nitrophenyl-beta-D-mannoside


organism: Cyamopsis tetragonoloba

substrate_name: p-nitrophenyl-beta-D-mannopyranoside; 4-methylumbelliferyl beta-D-mannopyranoside; o-nitrophenyl-beta-D-mannopyranoside; beta-D-mannotetraitol; Beta-D-mannohexaitol; beta-D-mannopentaitol; beta-D-mannotriitol


organism: Gallus gallus


enzyme_display_name: sugar-phosphatase

organism: Arabidopsis thaliana

substrate_name: 2-deoxy-D-glucose 6-phosphate

sequence_source: UniProt Q9ZVJ5 FASTA/API direct accession lookup

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp', substrate row '2-deoxy-d-glucose-6-phosphate' = (3.3 ± 0.1) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (4.6 ± 0.5) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 7.2 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.3 x 10^1 s^-1; 3.3 x 10^1 = 33 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 33 s^(-1). Km: printed Table 1 cell 4.6 x 10^-3 M; 1 M is 1000 mM, so 4.6 x 10^-3 x 1000 = 4.6 mM; the exported value is 4.6 mM. kcat/Km: printed Table 1 cell 7.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.2 x 10^3 / 1000 = 7.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '2-deoxy-d-glucose-6-phosphate', enzyme column 'AtSgpp': kcat = 3.3 x 10^1 s^-1; Km = 4.6 x 10^-3 M; printed kcat/Km = 7.2 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2-deoxy-d-glucose-6-phosphate', enzyme column 'AtSgpp' (wild-type phosphosugar phosphatase AtSgpp)

table_label: Table 1: Kinetic parameter kcat, Km and kcat/Km of the phosphatase activity of purified AtSgpp and mutant proteins, on various organic phosphomonoesters (Planta 2014, 240:479-487)

enzyme: sugar-phosphatase

substrate: 2-deoxy-D-glucose 6-phosphate


substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProt Q9ZVJ5 canonical sequence, reconstructed by applying A69M from PMID 24915748 motif-5 mutation evidence and applied mutation signature A69M to reconstruct the assayed variant sequence.

substrate: D-glucose 6-phosphate


substrate_name: D-Mannose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProt Q9ZVJ5 canonical sequence, reconstructed by applying I68M from PMID 24915748 motif-5 mutation evidence and applied mutation signature I68M to reconstruct the assayed variant sequence.

substrate: D-Mannose 6-phosphate


substrate_name: D-Fructose 6-phosphate

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp', substrate row 'd-fructose-6-phosphate' = (1.9 ± 0.2) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (7.7 ± 0.4) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 2.5 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.9 x 10^1 s^-1; 1.9 x 10^1 = 19 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 19 s^(-1). Km: printed Table 1 cell 7.7 x 10^-3 M; 1 M is 1000 mM, so 7.7 x 10^-3 x 1000 = 7.7 mM; the exported value is 7.7 mM. kcat/Km: printed Table 1 cell 2.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^3 / 1000 = 2.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-fructose-6-phosphate', enzyme column 'AtSgpp': kcat = 1.9 x 10^1 s^-1; Km = 7.7 x 10^-3 M; printed kcat/Km = 2.5 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-fructose-6-phosphate', enzyme column 'AtSgpp' (wild-type phosphosugar phosphatase AtSgpp)

substrate: D-Fructose 6-phosphate


column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp', substrate row 'd-mannose-6-phosphate' = (3.2 ± 0.6) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (4.9 ± 0.6) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 6.7 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.2 x 10^1 s^-1; 3.2 x 10^1 = 32 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 32 s^(-1). Km: printed Table 1 cell 4.9 x 10^-3 M; 1 M is 1000 mM, so 4.9 x 10^-3 x 1000 = 4.9 mM; the exported value is 4.9 mM. kcat/Km: printed Table 1 cell 6.7 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.7 x 10^3 / 1000 = 6.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-mannose-6-phosphate', enzyme column 'AtSgpp': kcat = 3.2 x 10^1 s^-1; Km = 4.9 x 10^-3 M; printed kcat/Km = 6.7 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-mannose-6-phosphate', enzyme column 'AtSgpp' (wild-type phosphosugar phosphatase AtSgpp)


sequence_source: UniProt Q9ZVJ5 canonical sequence, reconstructed by applying A69M from PMID 24915748 motif-5 mutation evidence


column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp', substrate row 'd-glucose-6-phosphate' = (2.4 ± 0.5) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (7.1 ± 0.3) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 3.4 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.4 x 10^1 s^-1; 2.4 x 10^1 = 24 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 24 s^(-1). Km: printed Table 1 cell 7.1 x 10^-3 M; 1 M is 1000 mM, so 7.1 x 10^-3 x 1000 = 7.1 mM; the exported value is 7.1 mM. kcat/Km: printed Table 1 cell 3.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^3 / 1000 = 3.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-glucose-6-phosphate', enzyme column 'AtSgpp': kcat = 2.4 x 10^1 s^-1; Km = 7.1 x 10^-3 M; printed kcat/Km = 3.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-glucose-6-phosphate', enzyme column 'AtSgpp' (wild-type phosphosugar phosphatase AtSgpp)


substrate_name: decylubiquinone

proof_lines: mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication

substrate: decylubiquinone


proof_lines: mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W198A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W198A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W645A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W645A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


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

proof_lines: wild type enzyme, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q646A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q646A, at 37°C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as K71R and applied mutation signature K71R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as K71R


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as I68M and applied mutation signature I68M to reconstruct the assayed variant sequence.


substrate_name: DL-glycerol 3-phosphate

sequence_source: UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as I68M

substrate: DL-glycerol 3-phosphate


proof_lines: mutant enzyme K71R, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C


substrate_name: D-Ribose 5-phosphate

substrate: D-Ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as A69M and applied mutation signature A69M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as A69M


organism: Caldivirga maquilingensis

substrate_name: Sulfide

assay_conditions_summary: pH 7.5; 333.15 K; cofactor FAD

proof_lines: pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K

proof_lines: pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K


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


organism: Paracoccus denitrificans

proof_lines: in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication


organism: Pseudanabaena limnetica

proof_lines: in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C


proof_lines: wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication