sequence_source: UniProtKB P25500 displayed canonical sequence checked as identity context only; no row-specific variant sequence reconstructed.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 NIDNF216SIANS

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant His-tagged 1 Met-531

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant His-tagged 1 Met-503


enzyme_display_name: polynucleotide adenylyltransferase

organism: Bos taurus

substrate_name: ATP

source_db: oed

verification_status: unverified

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 UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature K228A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8.3; 310.15 K; cofactor ATP

data_origin: experimental

enzyme: polynucleotide adenylyltransferase

substrate: ATP

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature D208A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature V214Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature F100D to reconstruct the assayed variant sequence.


kcat_over_km_display: Not reported

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

sequence_source: UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature.

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 V214Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature R225A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 R225A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature H212A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 H212A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature E209A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 E209A


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 F100D

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant F100D


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 displayed canonical sequence; variant reconstructed by one-residue substitution from selected mutation_signature. and applied mutation signature N219A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 N219A


organism: Zea mays

substrate_name: TRIBOA glucoside

mutation_signature: Unknown

sequence_source: UniProtKB REST direct accession lookup for B1P123 on 2026-06-16

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

substrate: TRIBOA glucoside


enzyme_display_name: hyaluronan synthase

organism: Homo sapiens

substrate_name: UDP-D-glucosamine

source_db: brenda

kcat_display: Not reported

sequence_source: UniProtKB REST direct accession lookup for Q92819 on 2026-06-16

enzyme: hyaluronan synthase

substrate: UDP-D-glucosamine

source: brenda


sequence_source: UniProtKB REST direct accession lookup for O00219 on 2026-06-16


sequence_source: UniProtKB REST direct accession lookup for Q92839 on 2026-06-16


organism: Mus musculus

substrate_name: n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n UDPglucuronate

sequence_source: UniProtKB REST direct accession lookup for P70312 on 2026-06-16


sequence_source: UniProtKB REST direct accession lookup for Q61647 on 2026-06-16

substrate: n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n UDPglucuronate


substrate_name: n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_source: UniProtKB REST direct accession lookup for O08650 on 2026-06-16


organism: Pasteurella multocida

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D196E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D196E


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D196K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D196K


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D196N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D196N


substrate_name: beta-D-Glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-(nascent hyaluronan); n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D477E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D477E


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D477K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D477K

substrate: beta-D-Glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-(nascent hyaluronan); n n n n n n n n UDP-N-acetyl-D-glucosamine


substrate_name: n n n n n n n n UDP-N-acetyl-D-glucosamine; beta-D-Glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-(nascent hyaluronan)

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D477N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D477N


substrate_name: n n n n n n n n UDPglucuronate; n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16 and applied mutation signature D529E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant D529E


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

sequence_source: UniProtKB REST direct accession lookup for Q7BLV3 on 2026-06-16

proof_lines: with UDP-alpha-N-acetyl-D-glucosamine, pH 8.0, 35°C, recombinant enzyme

proof_lines: with UDP-alpha-D-glucuronate, pH 8.0, 35°C, recombinant enzyme

proof_lines: pH 7.0, 25 °C, 10 mM MnCl2 and 15 mM UDP-GlcNAc (in absence of HA oligosaccharide as acceptor substrate)

substrate: n n n n n n n n UDPglucuronate; n n n n n n n n UDP-N-acetyl-D-glucosamine


organism: Streptococcus equisimilis

substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_source: UniProtKB O50201 REST/FASTA direct lookup on 2026-06-16; canonical accession sequence.

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


organism: Streptococcus pyogenes

substrate_name: UDPglucuronate

sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C366S to reconstruct the assayed variant sequence.

substrate: UDPglucuronate


sequence_source: UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present.


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C124A/C225A/C261A/C280A/C366A/C402A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C124A/C225A/C261A/C280A/C366A/C402A


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate

sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C225S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C225S


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C124A/C366A/C402A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C124A/C366A/C402A

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C261A/C280A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C124A/C402A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C124A/C402A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C280S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C280S

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C124A/C261A/C280A/C366A/C402A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C261A/C280A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C366A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C366A


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C124A/C261A/C280A/C366A/C402A


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C366S


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C280A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 REST/FASTA direct lookup on 2026-06-16; canonical sequence with selected mutation signature applied when present. and applied mutation signature C225A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C225A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 direct lookup on 2026-06-16; selected mutation C261S applied to canonical sequence and applied mutation signature C261S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 direct lookup on 2026-06-16; selected mutation C366A applied to canonical sequence and applied mutation signature C366A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 direct lookup on 2026-06-16; selected mutation C280A applied to canonical sequence and applied mutation signature C280A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C280A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 direct lookup on 2026-06-16; selected mutation C124A applied to canonical sequence and applied mutation signature C124A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C124A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C0H0 direct lookup on 2026-06-16; selected mutation C225S applied to canonical sequence and applied mutation signature C225S to reconstruct the assayed variant sequence.


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate

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


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine


substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate


substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine


substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate


sequence_source: UniProtKB P0C0H0 direct lookup on 2026-06-16

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

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate


enzyme_display_name: D-histidine 2-aminobutanoyltransferase

organism: Staphylococcus aureus

substrate_name: D-histidine

sequence_source: UniProtKB A0A0H3JXA8 direct lookup on 2026-06-16

enzyme: D-histidine 2-aminobutanoyltransferase

substrate: D-histidine


substrate_name: ATP; n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n RNA (poly(A))

sequence_source: UniProtKB P25500 direct lookup on 2026-06-16


enzyme_display_name: fumigaclavine B O-acetyltransferase

organism: Aspergillus fumigatus

substrate_name: Fumigaclavine B; Acetyl-CoA

sequence_source: UniProtKB Q4WZ64 FASTA direct lookup on 2026-06-16

assay_conditions_summary: 310.15 K; cofactor CoA

proof_lines: pH not specified in the publication, 37°C, recombinant His6-tagged enzyme

enzyme: fumigaclavine B O-acetyltransferase

substrate: Fumigaclavine B; Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C124A/C402A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C402S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C402S


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C402A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C225A to reconstruct the assayed variant sequence.


sequence_source: Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C402A


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C124A/C366A/C402A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C261A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C261A


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C124A/C225A/C261A/C280A/C366A/C402A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C124S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C124A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C261S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C261S


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C124S


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P0C0H0 FASTA direct lookup on 2026-06-16 and applied mutation signature C280S to reconstruct the assayed variant sequence.


substrate_name: ATP

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 P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature R199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature D167N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature V154A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant V154A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature N202A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature D167N/N202A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant D167N/N202A


sequence_source: UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant R199A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature D167N/T317G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature Q323A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant Q323A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature K158A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant K158A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature N239A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant N239A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature K232A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature V247A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant V247A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 canonical FASTA reconstructed with selected mutation signature and applied mutation signature V156A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P25500, reviewed entry, checked 2026-06-16 and applied mutation signature V247A to reconstruct the assayed variant sequence.


substrate_name: n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n RNA (poly(A)); ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P25500, reviewed entry, checked 2026-06-16 and applied mutation signature F153A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant F153A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P25500, reviewed entry, checked 2026-06-16 and applied mutation signature V206A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant V206A

substrate: n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n RNA (poly(A)); ATP


sequence_source: UniProtKB REST accession P25500, reviewed entry, checked 2026-06-16


substrate_name: ATP; n+1 n n+1 n RNA (poly(A))

sequence_source: UniProtKB REST accession Q9BWT3, reviewed entry, checked 2026-06-16

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

substrate: ATP; n+1 n n+1 n RNA (poly(A))


substrate_name: n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n RNA (poly(A)); ATP

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: polynucleotide adenylyltransferase(Enzyme) mutant PAPgamma(H1-506), N-terminal His-tag

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant PAPgamma(H1-493), N-terminal His-tag


substrate_name: ATP; n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n RNA (poly(A))

sequence_source: UniProtKB REST accession P51003, reviewed entry, checked 2026-06-16


substrate_name: RNA (poly(A)); ATP

sequence_source: UniProtKB REST accession Q9NVV4, reviewed entry, checked 2026-06-16

substrate: RNA (poly(A)); ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q8NDF8, reviewed entry, checked 2026-06-16 and applied mutation signature K560E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession Q8NDF8, reviewed entry, checked 2026-06-16

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; 310.15 K; cofactor ATP


mutation_signature: C-terminal deletion mutant

mutation_type: deletion

proof_lines: C-terminal deletion mutant, pH 7.5, 37°C

substrate: ATP


substrate_name: ATP; RNA

sequence_source: UniProtKB REST accession Q9H6E5, reviewed entry, checked 2026-06-16

substrate: ATP; RNA


organism: Saccharomyces cerevisiae

substrate_name: 2-aminopurine riboside triphosphate

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

sequence_source: UniProtKB REST accession P29468, reviewed entry, checked 2026-06-16

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

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

source_databases_merged: brenda skid

substrate: 2-aminopurine riboside triphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P29468, reviewed entry, checked 2026-06-16 and applied mutation signature N189A to reconstruct the assayed variant sequence.


enzyme_display_name: cruzipain

organism: Trypanosoma cruzi

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: cruzipain(Enzyme) wildtype delta c (truncated wildtype)

enzyme: cruzipain


mutation_signature: truncated enzyme truncated enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature A319R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature D167N/T317G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant D167N/T317G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature K232A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant K232A

substrate: ATP; n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n RNA (poly(A))


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature D167N/N202A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature T317G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant T317G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature N239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature K158A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant A319R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature N202A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant N202A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature V247R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature D167N/V247R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant D167N/V247R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature D167N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant D167N


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant V247R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature V206A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 canonical sequence with row-specific mutation reconstruction and applied mutation signature V156A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant V156A


substrate_name: UDP-Glc-NAc (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2)

source_db: uniprot

source: uniprot


substrate: UDP-Glc-NAc (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2)


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


enzyme_display_name: Phosphite dehydrogenase

organism: Stutzerimonas stutzeri

substrate_name: phosphonate

sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature E266Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines:
pH 7.5, 25°C, E266Q mutant enzyme
mutant E266Q

enzyme: Phosphite dehydrogenase

substrate: phosphonate


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature K76A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 25°C, K76A mutant enzyme
mutant K76A


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature K76M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature K76C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature R237K to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 25°C, R237K mutant enzyme
mutant R237K


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature K76R to reconstruct the assayed variant sequence.


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence with row-specific mutation reconstruction and applied mutation signature Q137R/I150F/Q215L/R275Q/D162N/V315A to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q132R/Q137R/I150F/Q215L/R275Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 298.15 K; buffer pH carried to one decimal; cofactor NAD+

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 5x: column 'kcat (min^-1)' = 170; column 'Km (uM, NAD)' = 46; column 'kcat/Km,NAD (uM^-1 min^-1)' = 3.7; column 'Km (uM, Pt-H)' = 75.

normalized_value_unit_evidence: kcat: printed Table 2 cell 170 min^-1; 170 / 60 = 2.8333333333333335 s^-1; the exported value is 2.8 s^(-1). Km: printed Table 2 cell 46 uM; 46 / 1000 = 0.046 mM; the exported value is 0.046 mM. kcat/Km: printed Table 2 cell 3.7 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 3.7 * 1000 / 60 = 61.666666666666664 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 5x: kcat = 170 min^-1; Km (NAD) = 46 uM; printed kcat/Km,NAD = 3.7 uM^-1 min^-1; Km (Pt-H) = 75 uM.

row_label: Table 2, variant row 5x

table_label: Table 2: Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C (Appl. Environ. Microbiol. 2005, 71(10):5728-5734)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q132R to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 1-23C7: column 'kcat (min^-1)' = 238; column 'Km (uM, NAD)' = 60; column 'kcat/Km,NAD (uM^-1 min^-1)' = 4.0; column 'Km (uM, Pt-H)' = 45.

normalized_value_unit_evidence: kcat: printed Table 2 cell 238 min^-1; 238 / 60 = 3.966666666666667 s^-1; the exported value is 3.96 s^(-1). Km: printed Table 2 cell 60 uM; 60 / 1000 = 0.06 mM; the exported value is 0.045 mM. kcat/Km: printed Table 2 cell 4.0 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 4.0 * 1000 / 60 = 66.66666666666667 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 1-23C7: kcat = 238 min^-1; Km (NAD) = 60 uM; printed kcat/Km,NAD = 4.0 uM^-1 min^-1; Km (Pt-H) = 45 uM.

row_label: Table 2, variant row 1-23C7


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 12x: column 'kcat (min^-1)' = 195; column 'Km (uM, NAD)' = 40; column 'kcat/Km,NAD (uM^-1 min^-1)' = 4.9; column 'Km (uM, Pt-H)' = 46.

normalized_value_unit_evidence: kcat: printed Table 2 cell 195 min^-1; 195 / 60 = 3.25 s^-1; the exported value is 3.2 s^(-1). Km: printed Table 2 cell 40 uM; 40 / 1000 = 0.04 mM; the exported value is 0.04 mM. kcat/Km: printed Table 2 cell 4.9 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 4.9 * 1000 / 60 = 81.66666666666667 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 12x: kcat = 195 min^-1; Km (NAD) = 40 uM; printed kcat/Km,NAD = 4.9 uM^-1 min^-1; Km (Pt-H) = 46 uM.

row_label: Table 2, variant row 12x


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature I150F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 1-25E8: column 'kcat (min^-1)' = 262; column 'Km (uM, NAD)' = 75; column 'kcat/Km,NAD (uM^-1 min^-1)' = 3.5; column 'Km (uM, Pt-H)' = 99.

normalized_value_unit_evidence: kcat: printed Table 2 cell 262 min^-1; 262 / 60 = 4.366666666666666 s^-1; the exported value is 4.4 s^(-1). Km: printed Table 2 cell 75 uM; 75 / 1000 = 0.075 mM; the exported value is 0.075 mM. kcat/Km: printed Table 2 cell 3.5 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 3.5 * 1000 / 60 = 58.333333333333336 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 1-25E8: kcat = 262 min^-1; Km (NAD) = 75 uM; printed kcat/Km,NAD = 3.5 uM^-1 min^-1; Km (Pt-H) = 99 uM.

row_label: Table 2, variant row 1-25E8


enzyme_display_name: phosphite dehydrogenase

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB O69054/PTXD_STUST canonical sequence after direct EC+organism lookup; mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R was validated at each O69054 residue position. and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R to reconstruct the assayed variant sequence.

enzyme: phosphite dehydrogenase


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB O69054/PTXD_STUST canonical sequence after direct EC+organism lookup; mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A was validated at each O69054 residue position. and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 1-1A9: column 'kcat (min^-1)' = 285; column 'Km (uM, NAD)' = 66; column 'kcat/Km,NAD (uM^-1 min^-1)' = 4.3; column 'Km (uM, Pt-H)' = 48.

normalized_value_unit_evidence: kcat: printed Table 2 cell 285 min^-1; 285 / 60 = 4.75 s^-1; the exported value is 4.75 s^(-1). Km: printed Table 2 cell 66 uM; 66 / 1000 = 0.066 mM; the exported value is 0.048 mM. kcat/Km: printed Table 2 cell 4.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 4.3 * 1000 / 60 = 71.66666666666667 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 1-1A9: kcat = 285 min^-1; Km (NAD) = 66 uM; printed kcat/Km,NAD = 4.3 uM^-1 min^-1; Km (Pt-H) = 48 uM.

row_label: Table 2, variant row 1-1A9


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 3-135H2: column 'kcat (min^-1)' = 213; column 'Km (uM, NAD)' = 50; column 'kcat/Km,NAD (uM^-1 min^-1)' = 4.3; column 'Km (uM, Pt-H)' = 135.

normalized_value_unit_evidence: kcat: printed Table 2 cell 213 min^-1; 213 / 60 = 3.55 s^-1; the exported value is 3.5 s^(-1). Km: printed Table 2 cell 50 uM; 50 / 1000 = 0.05 mM; the exported value is 0.05 mM. kcat/Km: printed Table 2 cell 4.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 4.3 * 1000 / 60 = 71.66666666666667 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 3-135H2: kcat = 213 min^-1; Km (NAD) = 50 uM; printed kcat/Km,NAD = 4.3 uM^-1 min^-1; Km (Pt-H) = 135 uM.

row_label: Table 2, variant row 3-135H2


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB O69054/PTXD_STUST canonical sequence after direct EC+organism lookup; mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I was validated at each O69054 residue position. and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 3-110G7: column 'kcat (min^-1)' = 216; column 'Km (uM, NAD)' = 71; column 'kcat/Km,NAD (uM^-1 min^-1)' = 3.0; column 'Km (uM, Pt-H)' = 156.

normalized_value_unit_evidence: kcat: printed Table 2 cell 216 min^-1; 216 / 60 = 3.6 s^-1; the exported value is 3.5 s^(-1). Km: printed Table 2 cell 71 uM; 71 / 1000 = 0.071 mM; the exported value is 0.071 mM. kcat/Km: printed Table 2 cell 3.0 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 3.0 * 1000 / 60 = 50.0 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 3-110G7: kcat = 216 min^-1; Km (NAD) = 71 uM; printed kcat/Km,NAD = 3.0 uM^-1 min^-1; Km (Pt-H) = 156 uM.

row_label: Table 2, variant row 3-110G7


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 3-89D3: column 'kcat (min^-1)' = 216; column 'Km (uM, NAD)' = 75; column 'kcat/Km,NAD (uM^-1 min^-1)' = 2.9; column 'Km (uM, Pt-H)' = 123.

normalized_value_unit_evidence: kcat: printed Table 2 cell 216 min^-1; 216 / 60 = 3.6 s^-1; the exported value is 3.5 s^(-1). Km: printed Table 2 cell 75 uM; 75 / 1000 = 0.075 mM; the exported value is 0.075 mM. kcat/Km: printed Table 2 cell 2.9 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 2.9 * 1000 / 60 = 48.333333333333336 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 3-89D3: kcat = 216 min^-1; Km (NAD) = 75 uM; printed kcat/Km,NAD = 2.9 uM^-1 min^-1; Km (Pt-H) = 123 uM.

row_label: Table 2, variant row 3-89D3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q215L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 1-11A6: column 'kcat (min^-1)' = 278; column 'Km (uM, NAD)' = 64; column 'kcat/Km,NAD (uM^-1 min^-1)' = 4.3; column 'Km (uM, Pt-H)' = 58.

normalized_value_unit_evidence: kcat: printed Table 2 cell 278 min^-1; 278 / 60 = 4.633333333333334 s^-1; the exported value is 4.6 s^(-1). Km: printed Table 2 cell 64 uM; 64 / 1000 = 0.064 mM; the exported value is 0.058 mM. kcat/Km: printed Table 2 cell 4.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 4.3 * 1000 / 60 = 71.66666666666667 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 1-11A6: kcat = 278 min^-1; Km (NAD) = 64 uM; printed kcat/Km,NAD = 4.3 uM^-1 min^-1; Km (Pt-H) = 58 uM.

row_label: Table 2, variant row 1-11A6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R/I150F/Q215L/R275Q/A319E to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 2-9B6: column 'kcat (min^-1)' = 198; column 'Km (uM, NAD)' = 52; column 'kcat/Km,NAD (uM^-1 min^-1)' = 3.8; column 'Km (uM, Pt-H)' = 92.

normalized_value_unit_evidence: kcat: printed Table 2 cell 198 min^-1; 198 / 60 = 3.3 s^-1; the exported value is 3.2 s^(-1). Km: printed Table 2 cell 52 uM; 52 / 1000 = 0.052 mM; the exported value is 0.052 mM. kcat/Km: printed Table 2 cell 3.8 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 3.8 * 1000 / 60 = 63.333333333333336 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 2-9B6: kcat = 198 min^-1; Km (NAD) = 52 uM; printed kcat/Km,NAD = 3.8 uM^-1 min^-1; Km (Pt-H) = 92 uM.

row_label: Table 2, variant row 2-9B6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature R275Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 1-8D6: column 'kcat (min^-1)' = 244; column 'Km (uM, NAD)' = 70; column 'kcat/Km,NAD (uM^-1 min^-1)' = 3.5; column 'Km (uM, Pt-H)' = 78.

normalized_value_unit_evidence: kcat: printed Table 2 cell 244 min^-1; 244 / 60 = 4.066666666666666 s^-1; the exported value is 4.1 s^(-1). Km: printed Table 2 cell 70 uM; 70 / 1000 = 0.07 mM; the exported value is 0.07 mM. kcat/Km: printed Table 2 cell 3.5 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 3.5 * 1000 / 60 = 58.333333333333336 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 1-8D6: kcat = 244 min^-1; Km (NAD) = 70 uM; printed kcat/Km,NAD = 3.5 uM^-1 min^-1; Km (Pt-H) = 78 uM.

row_label: Table 2, variant row 1-8D6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Q137R/I150F/Q215L/R275Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the parent and evolved PTDH variants in 50 mM MOPS (pH 7.25) at 25 C), variant row 4x: column 'kcat (min^-1)' = 218; column 'Km (uM, NAD)' = 74; column 'kcat/Km,NAD (uM^-1 min^-1)' = 2.9; column 'Km (uM, Pt-H)' = 144.

normalized_value_unit_evidence: kcat: printed Table 2 cell 218 min^-1; 218 / 60 = 3.6333333333333333 s^-1; the exported value is 3.6 s^(-1). Km: printed Table 2 cell 74 uM; 74 / 1000 = 0.074 mM; the exported value is 0.074 mM. kcat/Km: printed Table 2 cell 2.9 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and 1 min^-1 is 1/60 s^-1, so 2.9 * 1000 / 60 = 48.333333333333336 s^-1 mM^-1; the catalog row stores no catalytic-efficiency value, so the printed efficiency cell is carried here as typed primary_reported provenance only.

raw_value_unit_evidence: Table 2, variant row 4x: kcat = 218 min^-1; Km (NAD) = 74 uM; printed kcat/Km,NAD = 2.9 uM^-1 min^-1; Km (Pt-H) = 144 uM.

row_label: Table 2, variant row 4x


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB O69054/PTXD_STUST canonical sequence after direct EC+organism lookup; mutation signature D13E/M26I/E175A/T181S/A308T/E332N/C336D was validated at each O69054 residue position. and applied mutation signature D13E/M26I/E175A/T181S/A308T/E332N/C336D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADP+

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E175A/T181S/A308T/E332N/C336D, pH 7.3, 25°C


organism: Methylorubrum extorquens

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


organism: Ralstonia sp. 4506

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping; variant reconstructed from selected mutation signature after residue check. and applied mutation signature C174H/D175A/P176R/I177K/P178A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NADP+

proof_lines: pH 7.3, 37°C, recombinant His-tagged mutant C174H/D175A/P176R/I177K/P178A

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping; variant reconstructed from selected mutation signature after residue check. and applied mutation signature C174H/D175A/P176R/I177R/P178A to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 37°C, recombinant His-tagged mutant C174H/D175A/P176R/I177R/P178A


sequence_variant_note: Resolved canonical sequence from UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping; variant reconstructed from selected mutation signature after residue check. and applied mutation signature D175A/P176R to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 37°C, recombinant His-tagged mutant D175A/P176R


sequence_source: UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping.

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

proof_lines: pH 7.3, 37°C, recombinant His-tagged wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping; variant reconstructed from selected mutation signature after residue check. and applied mutation signature C174H/D175A/P176R to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 37°C, recombinant His-tagged mutant C174H/D175A/P176R


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

assay_conditions_summary: pH 7.25; 298.15 K; cofactor NADP+


proof_lines: cosubstrate NADP+, mutant E175A, pH 7.3, 25°C


proof_lines: 25°C, pH 7.25, E175A/A176R mutant enzyme


sequence_source: UniProtKB reviewed O69054/PTXD_STUST direct EC+organism lookup.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines:
pH 7.5, 25°C, wild type enzyme
wild-type, pH 7.3, 25°C
wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature K330* to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NAD+, mutant K330*, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D13E/M26I/E175A/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature M26I/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NAD+, mutant M26I/E332N/C336D, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D13E/M26I/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D13E/M26I/E175A/T181S/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C


substrate_name: phosphite

sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D79N to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

substrate: phosphite


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D79A to reconstruct the assayed variant sequence.


km_display: Not reported

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

proof_lines:
mutant NADP-12X NAD
thermostable mutant 12X-PTDH


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Vitis vinifera

substrate_name: D-glyceraldehyde 3-phosphate

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: D-glyceraldehyde 3-phosphate


organism: Badhamia polycephala

substrate_name: putrescine

substrate: putrescine


proof_lines: kcat is 0.249 sec(-1) for TRIBOA-glucoside.


organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)

substrate_name: D-histidine

substrate: D-histidine


substrate_name: UTP

proof_lines: kcat is 0.059 sec(-1) with UTP as substrate. kcat is 0.002 sec(-1) with ATP as substrate. kcat is 0.061 sec(-1) with U6 snRNA-u4 as substrate.

substrate: UTP


enzyme_display_name: protein-serine/threonine phosphatase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: pNPP

proof_lines: kcat is 0.0076 sec(-1) with pNPP as substrate.

enzyme: protein-serine/threonine phosphatase

substrate: pNPP


organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

proof_lines: kcat is 0.00162 sec(-1) with pNPP as substrate.


enzyme_display_name: nicotinamidase

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

substrate_name: nicotinamide

enzyme: nicotinamidase

substrate: nicotinamide


organism: Arabidopsis thaliana

proof_lines: kcat is 0.93 sec(-1) with nicotinamide as substrate.


substrate_name: CTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P29468 canonical FASTA fetched 2026-06-16 plus selected mutation_signature Y224F and applied mutation signature Y224F to reconstruct the assayed variant sequence.

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29468 canonical FASTA fetched 2026-06-16 plus selected mutation_signature N226A and applied mutation signature N226A to reconstruct the assayed variant sequence.


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P29468 canonical FASTA fetched 2026-06-16 plus selected mutation_signature K215A and applied mutation signature K215A to reconstruct the assayed variant sequence.

substrate: ATP


substrate_name: GTP

sequence_source: UniProtKB:P29468 canonical FASTA fetched 2026-06-16

substrate: GTP


sequence_source: UniProtKB:Q598P5 canonical FASTA fetched 2026-06-16

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

proof_lines: recombinant form without C-terminal extension


sequence_source: UniProtKB:P25779 canonical FASTA fetched 2026-06-16

proof_lines: 37°C, pH 5.5, recombinant cruzain, consisting of the catalytic domain of cruzipain but excluding the carboxy-terminal extension

proof_lines: pH and temperature not specified in the publication


substrate_name: Benzoyl-Pro-Phe-Arg-p-nitroanilide

substrate: Benzoyl-Pro-Phe-Arg-p-nitroanilide


proof_lines:
pH 8.5, 25°C, wild-type enzyme
pH 5.5, 25°C, wild-type enzyme
pH 3.5, 25°C, wild-type enzyme


organism: Pagrus major

substrate_name: CBz-Gln-Ser

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

substrate: CBz-Gln-Ser


organism: Patinopecten sp.

substrate_name: Monodansylcadaverine

proof_lines:
pH 7.5, 10°C, hemocyte enzyme
pH 7.5, 10°C, muscle enzyme

substrate: Monodansylcadaverine


organism: Rattus norvegicus

substrate_name: methylamine

proof_lines:
chondrosarcoma transglutaminase B
soluble liver transglutaminase
brain transglutaminase NI

substrate: methylamine


organism: Streptomyces hygroscopicus

substrate_name: N-carboxybenzoyl-L-glutaminyl-glycine

proof_lines:
recombinant enzyme, at pH 8.0 and 37°C
pH 6.0, 37°C
native enzyme, at pH 8.0 and 37°C

substrate: N-carboxybenzoyl-L-glutaminyl-glycine


organism: Streptomyces mobaraensis

substrate_name: Propylamine

assay_conditions_summary: pH 8; 310.15 K; buffer 250 mM Tris acetate

proof_lines: 1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5-N,N-dimethylamino-1-naphthalenesulfonyl)diamidopentane as glutamine donor

proof_lines: 1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5-N-N-dimethylamino-1naphthalenesulfonyl)diamidopentane as glutamine donor

proof_lines: in 250 mM Tris acetate buffer (pH 8.0), at 37°C

substrate: Propylamine


organism: Streptomyces sp. TYQ1024

substrate_name: CBz-Gln-Gly

substrate: CBz-Gln-Gly


substrate_name: UDPglucose

substrate: UDPglucose


organism: Brassica napus

substrate_name: phenylacetothiohydroximate

substrate: phenylacetothiohydroximate


organism: Tropaeolum majus

proof_lines: pH 7.4, 30°C, phenylacetothiohydroximate

proof_lines: pH 7.4, 30°C, 4-methylthiobutyrothiohydroximate


organism: Candidatus Mycoplasma liparidae

substrate_name: UDP-D-glucosamine

substrate: UDP-D-glucosamine


organism: Mus musculus

substrate_name: UDP-D-glucuronate

substrate: UDP-D-glucuronate


organism: Bos taurus

substrate_name: putrescine

proof_lines: tissue transglutaminase from endothelial cells

substrate: putrescine


organism: Cavia porcellus

proof_lines:
transglutaminase C
pH 7.4, 30°C
native enzyme


organism: Gallus gallus

substrate_name: casein

proof_lines:
gizzard transglutaminase
plasma factor XII, actin

substrate: casein


organism: Glycine max


organism: Homo sapiens

substrate_name: NQENVSPLTLLRLGN

proof_lines:
37°C, pH 7.4
recombinant transglutaminase 5
factor XIIIa

substrate: NQENVSPLTLLRLGN


substrate_name: Nalpha-benzyloxycarbonyl-L-Gln-Gly

proof_lines: Km above 0.03 mM, mutant enzyme C371A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C

substrate: Nalpha-benzyloxycarbonyl-L-Gln-Gly


proof_lines: Km above 0.03 mM, mutant enzyme C370A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C


proof_lines: wild type enzyme, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C


proof_lines: mutant enzyme C230A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C


organism: Lathyrus oleraceus


proof_lines: enzyme induced by 12-O-tetradecanoylphorbol-13-acetate or Ca2+


organism: Mythimna separata

substrate_name: N-Cbz-Gln-Gly

substrate: N-Cbz-Gln-Gly


organism: Streptococcus dysgalactiae subsp. equisimilis

substrate_name: UDP-N-acetyl-D-glucosamine

proof_lines: pH 7.0, 30°C, recombinant mutant C262A/C367A

substrate: UDP-N-acetyl-D-glucosamine


proof_lines: pH 7.0, 30°C, recombinant mutant C226A/C367A


organism: Streptococcus equisimilis

substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262A, C281A


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A, C367A

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C281S


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A, C262A

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C367A


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant (3C)C226

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant (3C)C262

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant (3C)C281


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C367S


organism: Pasteurella multocida


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C226A/C262A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C226A/C262A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C262A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:O50201 / NCBI Protein:AAB87874.1

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

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C281A/C367A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C281A/C367A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C226A/C281A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C226A/C281A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C226S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C262S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C367A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C281S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C367S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C262A/C281A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C262A/C281A


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature A319R to reconstruct the assayed variant sequence.

substrate: ATP


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature Y237A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature G203H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature R199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature K232A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature V247R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature D167N/T317G to reconstruct the assayed variant sequence.


sequence_source: RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500

assay_conditions_summary: 310.15 K; buffer formamide; cofactor ATP

proof_lines: wild-type, reactions are started with the addition of PAP and incubated at 37 °C for 15 minutes. Reactions are stopped by the addition of 8 microL of stop buffer (formamide with trace amount of bromophenol blue dye)


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature K158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature T317G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature N239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature K228A to reconstruct the assayed variant sequence.


organism: Xenopus laevis

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


proof_lines: pH 7.5, 30°C, recombinant mutant C337S at higher UDP-glucuronate concentration


proof_lines: pH 7.5, 30°C, recombinant mutant C239S/C337S


proof_lines: pH 7.5, 30°C, recombinant mutant C304S/C337S


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, recombinant wild-type enzyme at low UDP-glucuronate concentration

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme at low UDP-N-acetyl-D-glucosamine concentration, and mutant C239S

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme and mutants C210S, C337S at low UDP-glucuronate concentration


enzyme_display_name: thymidine phosphorylase

organism: Escherichia coli

assay_conditions_summary: pH 6.5; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: in 0.1 M potassium phosphate buffer (pH 7.4), at 25°C

enzyme: thymidine phosphorylase


substrate_name: thymidine

proof_lines:
normal tissue
37°C, pH 7.4
tumor tissue

substrate: thymidine


organism: Lacticaseibacillus casei

substrate_name: phosphate

substrate: phosphate


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C226A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate

sequence_source: UniProt REST O50201 canonical sequence; checked 2026-06-16.

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


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C262A/C367A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262A, C367A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C281A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C281A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C262A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C262S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262S


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C281A/C367A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C281A, C367A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C226S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226S


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C226A/C281A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A, C281A


organism: Streptococcus pyogenes


proof_lines: pH 7.5, 30°C, recombinant mutants C117S and C210S


enzyme_display_name: tRNA uracil 4-sulfurtransferase

organism: Bacillus subtilis

substrate_name: L-cysteine

enzyme: tRNA uracil 4-sulfurtransferase

substrate: L-cysteine


proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, sulfur deficient tRNA
pH 7.8, 37°C


enzyme_display_name: keratan sulfotransferase

substrate_name: Keratan sulfate

enzyme: keratan sulfotransferase

substrate: Keratan sulfate


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Aloe vera

substrate_name: S-acetylglutathione

enzyme: hydroxyacylglutathione hydrolase

substrate: S-acetylglutathione


organism: Candida albicans

substrate_name: S-D-lactoylglutathione

substrate: S-D-lactoylglutathione


organism: Cyberlindnera mrakii

substrate_name: S-Lactoylglutathione

substrate: S-Lactoylglutathione


proof_lines: recombinant wild-type enzyme, pH 7.1, 37°C


organism: Leishmania infantum

substrate_name: mono-(lactoyl)trypanothione

substrate: mono-(lactoyl)trypanothione


organism: Mus musculus


organism: Oryza sativa

proof_lines: pH and temperature not specified in the publication, Vmax: 1 mmol/min/mg


organism: Bos taurus

substrate_name: RNA (A)15

sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature D167N/N202A to reconstruct the assayed variant sequence.

substrate: RNA (A)15


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature F153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature V206A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature D167N/V247R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature N202A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature F100D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature V247A to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 9; 308.15 K; cofactor ATP

proof_lines: p(A)3 primer, Mn2+-activated calf thymus enzyme


organism: Cricetulus griseus


substrate_name: CTP

assay_conditions_summary: 303.15 K; cofactor ATP

substrate: CTP


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


organism: Mesocricetus auratus

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines:
polymerase IIb, 37°C
polymerase IIa, 37°C


organism: Rattus norvegicus

substrate_name: thymine

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

proof_lines: enzyme from SD-lymphoma, pH 6.4, 37°C, substrate: phosphate

proof_lines: enzyme from SD-lymphoma, pH 6.4, 37°C, substrate: 2-deoxythymidine

substrate: thymine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: arsenate

substrate: arsenate


enzyme_display_name: sym-norspermidine synthase

organism: Saccharolobus solfataricus

substrate_name: putrescine

enzyme: sym-norspermidine synthase

substrate: putrescine


enzyme_display_name: thermospermine synthase

organism: Thalassiosira pseudonana

substrate_name: spermidine

enzyme: thermospermine synthase

substrate: spermidine


organism: Yersinia pseudotuberculosis


enzyme_display_name: anhydro-N-acetylmuramic acid kinase

organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: in 100 mM Tris-HCl (pH 7.5), 20 mM MgCl2, at 37°C

enzyme: anhydro-N-acetylmuramic acid kinase


enzyme_display_name: polynucleotide adenylyltransferase

organism: Artemia sp.

substrate_name: dATP

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

enzyme: polynucleotide adenylyltransferase

substrate: dATP


organism: Bacillus subtilis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


assay_conditions_summary: cofactor ATP


organism: Pseudomonas putida

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate: ATP


organism: Saccharomyces cerevisiae

proof_lines: incubation at 30 °C for 15 min in the presence of MgATP2-


proof_lines:
wild-type PAP, incubation at 30 °C
wild-type PAP


organism: Triticum aestivum


organism: Vigna radiata


organism: Zea mays

substrate_name: Nucleotide

substrate: Nucleotide


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase

substrate_name: GTP

proof_lines: PhnI, PhnG, PhnH and PhnL, GST tags in situ removed, proteins begin to precipitate after removal of the GST tags, therefore kinetic constants are not definitive, pH not specified in the publication, temperature not specified in the publicat

proof_lines: PhnI, nucleosidase activity, pH not specified in the publication, temperature not specified in the publication

substrate: GTP


organism: Plasmodium falciparum

proof_lines: mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4


proof_lines: mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: inhibitor binding to the free enzyme, at 25°C, pH 6.8

proof_lines: inhibitor binding to the occupied enzyme, at 25°C, pH 6.8


proof_lines:
mitochondrial enzyme
enzyme from erythrocytes
matrix enzyme


substrate_name: S-D-mandeloylglutathione

substrate: S-D-mandeloylglutathione


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


assay_conditions_summary: pH 7.2; 298.15 K; buffer 10 mM MOPS

proof_lines: in 10 mM MOPS buffer at pH 7.2, at 25 °C


organism: Bacillus anthracis

substrate_name: 4-nitrophenyl phosphate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: 4-nitrophenyl phosphate


substrate_name: H2O; SpoIIAA-phosphorylated

substrate: H2O; SpoIIAA-phosphorylated


organism: Bos taurus

substrate_name: FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR

proof_lines:
30°C, AC dimer
30°C, C-subunit
30°C, AC-R2

substrate: FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR


organism: chicken anemia virus

substrate_name: RRApTVA

substrate: RRApTVA


organism: Enterococcus faecium

proof_lines: mutant enzyme T101R, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


proof_lines: mutant enzyme D136Y, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: mutant enzyme D136Y, with 0.05 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


proof_lines: mutant enzyme S120R, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: mutant enzyme S120R, with 0.05 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


proof_lines: wild type enzyme, with 0.05 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: wild type enzyme, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


substrate_name: 4-Nitrophenyl phosphate; H2O

substrate: 4-Nitrophenyl phosphate; H2O


organism: Glycine max

substrate_name: phosphohistone H1

substrate: phosphohistone H1


organism: Homo sapiens


proof_lines: pH 7.5, 30°C, recombinant His-tagged Wip1 catalytic subunit


organism: Hymenolepis diminuta

substrate_name: DLDVPIPGRFDRRVSVAAE

substrate: DLDVPIPGRFDRRVSVAAE


organism: Hymenolepis microstoma


organism: Lambdavirus lambda

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


proof_lines:
pH 7.8, wild-type Prep 2
pH 7.8, wild-type Prep 1


enzyme_display_name: oleoyl-[acyl-carrier-protein] hydrolase

organism: Arabidopsis thaliana

substrate_name: stearoyl-[acyl-carrier protein]

proof_lines:
isozyme FatB, pH 8.0, 22°C
isozyme FatA, pH 8.0, 22°C

enzyme: oleoyl-[acyl-carrier-protein] hydrolase

substrate: stearoyl-[acyl-carrier protein]


substrate_name: myristoyl-ACP (14:0-ACP)

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

proof_lines: The catalytic efficiency for 18:1 is at least 20-fold higher than for other substrates.

substrate: myristoyl-ACP (14:0-ACP)


organism: Escherichia coli (strain K12)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as


organism: Lathyrus oleraceus


organism: Meleagris gallopavo

substrate_name: heavy meromyosin

substrate: heavy meromyosin


organism: Oryctolagus cuniculus

substrate_name: phosphorylase a

proof_lines:
presence of Mn2+
absence of Mn2+

substrate: phosphorylase a


organism: Rattus norvegicus

substrate_name: Phosphoprotein; H2O

proof_lines: SABIO-RK modifier species: phosphoprotein phosphatase(Enzyme) mutant a/CaNA

substrate: Phosphoprotein; H2O


substrate_name: phosphohistone

substrate: phosphohistone


organism: Saccharomyces cerevisiae

proof_lines: purified, catalytically active 40 kDa-subunit, in 300 mM Tris pH 7.8, 150 mM potassium chloride, 25 mM magnesium chloride, 5 mM dithiothreitol, at 30°C

proof_lines: full-length Ppt1, in 300 mM Tris pH 7.8, 150 mM potassium chloride, 25 mM magnesium chloride, 5 mM dithiothreitol, at 30°C


organism: Salmonella enterica

substrate_name: serine/threonine-phosphorylated myelin basic protein

proof_lines:
pH 8.0, recombinant His-tagged enzyme
pH 9.5, recombinant His-tagged enzyme


organism: Synechocystis sp.

substrate_name: phosphoserine-myelin basic protein

proof_lines:
pH 7.5, 37°, recombinant SynPPP1
pH 7.5, 37°, recombinant SynPPM3

substrate: phosphoserine-myelin basic protein


organism: Triticum aestivum

substrate_name: phosphocasein

substrate: phosphocasein


organism: Trypanosoma brucei


enzyme_display_name: dGTPase

organism: Escherichia coli

substrate_name: dGTP

enzyme: dGTPase

substrate: dGTP


enzyme_display_name: glutamyl aminopeptidase

organism: Aspergillus oryzae

substrate_name: L-Leu-beta-naphthylamide

enzyme: glutamyl aminopeptidase

substrate: L-Leu-beta-naphthylamide


organism: Ricinus communis

substrate_name: oleoyl-[acyl-carrier protein]

smiles: CCCCCCCCC=CCCCCCCCC(=O)S

substrate: oleoyl-[acyl-carrier protein]


substrate_name: palmitoyl-[acyl-carrier protein]

sequence_source: UniProtKB:A9XK92 REST/FASTA direct lookup on 2026-06-16

assay_conditions_summary: pH 8; 295.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C

substrate: palmitoyl-[acyl-carrier protein]


substrate_name: palmitoleoyl-[acyl-carrier protein]

smiles: *SC(=O)CCCCCCC/C=C\CCCCCC

substrate: palmitoleoyl-[acyl-carrier protein]


sequence_source: UniProtKB:A9XUG5 REST/FASTA direct lookup on 2026-06-16


smiles: *SC(=O)CCCCCCCCCCCCCCC


smiles: *SC(=O)CCCCCCCCCCCCCCCCC


organism: Homo sapiens

substrate_name: acetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: acetyl-CoA


organism: Mus musculus

substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: Unknown

substrate: Unknown


substrate_name: UDP-xylose

assay_conditions_summary: pH 7; 310.15 K; buffer the batch. Source notes: in 100 mM cacodylate

proof_lines: in 100 mM cacodylate buffer, pH 7.0 containing 10 mM MnCl2 and 0.2-6 microM purified fusion-beta1,4-GalT7

proof_lines: recombinant maltose-binding protein-beta1,4-GalT7 fusion protein

substrate: UDP-xylose


substrate_name: UDP-galactose

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

assay_conditions_summary: pH 7; 310.15 K; buffer 100 mM sodium cacodylate

proof_lines: pH 7.0, 37°C, mutant D230A, protein expressed in HeLa cells

proof_lines: mutant enzyme D230A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C

substrate: UDP-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature G223A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant G223A, protein expressed in HeLa cells

proof_lines: mutant enzyme G223A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature W224H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature D165E to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant D165E, protein expressed in HeLa cells

proof_lines: mutant enzyme D165E, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature W222A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant W222A, protein expressed in HeLa cells

proof_lines: mutant enzyme W222A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature E227D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature F221Y to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant F221Y, protein expressed in HeLa cells

proof_lines: mutant enzyme F221Y, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature W222F to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant W222F, protein expressed in HeLa cells

proof_lines: mutant enzyme W222F, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature D228E to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant D228E, protein expressed in HeLa cells

proof_lines: mutant enzyme D228E, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


proof_lines: pH 7.0, 37°C, mutant W224H, protein expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, mutant W224H, protein expressed in HeLa cells

proof_lines: mutant enzyme W224H, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature F221A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant F221A, protein expressed in HeLa cells

proof_lines: mutant enzyme F221A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


proof_lines: pH 7.0, 37°C, mutant E227D, protein expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, mutant E227D, protein expressed in HeLa cells

proof_lines: mutant enzyme E227D, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature V164A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant V164A, protein expressed in HeLa cells

proof_lines: mutant enzyme V164A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


organism: Cuphea hookeriana

substrate_name: decanoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for Q39514 on 2026-06-16

smiles: *SC(=O)CCCCCCCCC

substrate: decanoyl-[acyl-carrier protein]


sequence_variant_note: Resolved canonical sequence from UniProtKB REST lookup for Q39514 on 2026-06-16 and applied mutation signature I198E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST lookup for Q39514 on 2026-06-16 and applied mutation signature K287E to reconstruct the assayed variant sequence.


substrate_name: dodecanoyl-[acyl-carrier protein]; octanoyl-[acyl-carrier protein]

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

proof_lines: acyl carrier protein of Escherichia coli, pH 8, temperature not specified in the publication

proof_lines: acyl carrier protein2 of Cuphea hookeriana, pH 8, temperature not specified in the publication


organism: Cuphea palustris

substrate_name: octanoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for Q39554 on 2026-06-16

proof_lines: at pH 7.4, temperature not specified in the publication

substrate: octanoyl-[acyl-carrier protein]


organism: Koelreuteria paniculata

substrate_name: palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for A0A678PVH0 on 2026-06-16


sequence_source: UniProtKB REST lookup for A0A7S5LEX2 on 2026-06-16

substrate: palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]


organism: Macadamia tetraphylla

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


substrate_name: palmitoleoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]; palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for D5FFZ2 on 2026-06-16


substrate_name: palmitoleoyl-[acyl-carrier protein]; palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for D2E6T0 on 2026-06-16


substrate_name: stearoyl-[acyl-carrier protein]

substrate: stearoyl-[acyl-carrier protein]


substrate_name: UDP-alpha-D-galactose

sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature H195R to reconstruct the assayed variant sequence.

substrate: UDP-alpha-D-galactose


sequence_source: UniProt REST/FASTA direct accession check

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

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

proof_lines: pH 7.0, 37°C, wild-type, protein expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, wild-type, protein expressed in HeLa cells


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature H195Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature R270K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; buffer 100 mm sodium cacodylate

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R270K; shared kcat column cell = 48.7 min^-1; 4-MUX Km column cell = 0.54 mm; 4-MUX kcat/Km column cell = 85 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 48.7 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 48.7 / 60 = 0.8116666666666668 s^-1; the exported value is 0.81 s^(-1). Km: printed Table 1 cell 0.54 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.54 mM; the exported value is 0.54 mM. kcat/Km: printed Table 1 cell 85 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 85 / 60 = 1.4166666666666667 s^-1 mM^-1; the exported value is 1.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270K, 4-MUX columns: kcat = 48.7 min^-1 (printed with its tolerance +/- 1.5); Km = 0.54 mm (printed with its tolerance +/- 0.07); kcat/Km = 85 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R270K; shared kcat column cell = 48.7 min^-1; UDP-Gal Km column cell = 0.37 mm; UDP-Gal kcat/Km column cell = 139 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 48.7 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 48.7 / 60 = 0.8116666666666668 s^-1; the exported value is 0.81 s^(-1). Km: printed Table 1 cell 0.37 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.37 mM; the exported value is 0.37 mM. kcat/Km: printed Table 1 cell 139 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 139 / 60 = 2.316666666666667 s^-1 mM^-1; the exported value is 2.1891891891891895 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270K, UDP-Gal columns: kcat = 48.7 min^-1 (printed with its tolerance +/- 1.5); Km = 0.37 mm (printed with its tolerance +/- 0.02); kcat/Km = 139 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature R226K to reconstruct the assayed variant sequence.


sequence_source: UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature R270A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R270A; shared kcat column cell = 46.4 min^-1; UDP-Gal Km column cell = 0.27 mm; UDP-Gal kcat/Km column cell = 184 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 46.4 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 46.4 / 60 = 0.7733333333333333 s^-1; the exported value is 0.77 s^(-1). Km: printed Table 1 cell 0.27 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.27 mM; the exported value is 0.27 mM. kcat/Km: printed Table 1 cell 184 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 184 / 60 = 3.066666666666667 s^-1 mM^-1; the exported value is 2.8518518518518516 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270A, UDP-Gal columns: kcat = 46.4 min^-1 (printed with its tolerance +/- 0.2); Km = 0.27 mm (printed with its tolerance +/- 0.01); kcat/Km = 184 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.