sequence_source: UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed E132A

proof_lines:
pH 5.0, 60°C, mutant E132A
pH 5.0, 20°C, mutant E132A


enzyme_display_name: protein-serine/threonine phosphatase

organism: Thermococcus kodakarensis

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 Q8X270 REST FASTA checked 2026-06-16; reconstructed Q136A and applied mutation signature Q136A to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: protein-serine/threonine phosphatase

status: unverified

source: oed


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed D63N/E132A and applied mutation signature D63N/E132A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 20°C, mutant D63N/E132A
pH 5.0, 60°C, mutant D63N/E132A

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed G95A and applied mutation signature G95A to reconstruct the assayed variant sequence.


mutation_signature: Unknown

sequence_source: UniProtKB Q8X270 REST FASTA checked 2026-06-16

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


proof_lines:
pH 5.0, 60°C, wild-type enzyme
pH 5.0, 20°C, wild-type enzyme


organism: Homo sapiens

substrate_name: p-nitrophenyl phosphate

source_db: uniprot

kcat_display: Not reported

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

substrate: p-nitrophenyl phosphate

source: uniprot


organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

substrate_name: MBP; EF-Tu

substrate: MBP; EF-Tu


organism: Mus musculus

substrate_name: a peptide

substrate: a peptide


organism: Oryctolagus cuniculus

substrate_name: phosphorylase

substrate: phosphorylase


organism: Rattus norvegicus

substrate_name: MAPT/TAU (at pH 7.4 and 30 degrees Celsius)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: p-nitrophenylphosphate

substrate: p-nitrophenylphosphate


substrate_name: phosphorylated CIT1

substrate: phosphorylated CIT1


organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

substrate_name: p-nitrophenylphosphate (at 30 degrees Celsius and at pH 7.4)


enzyme_display_name: cysteate synthase

organism: Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / CCUG 9716 / JCM 12966 / NCTC 12371 / SS31 / VPI 2845)

substrate_name: O-phospho-L-serine

sequence_source: source_record; accession cache; direct UniProt REST check 2026-06-16

proof_lines: kcat is 7.4 sec(-1) with O-phospho-L-serine as substrate. kcat is 11.9 sec(-1) with sulfite as substrate.

enzyme: cysteate synthase

substrate: O-phospho-L-serine


enzyme_display_name: thermospermine synthase

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

substrate_name: norspermidine (at pH 9 and 37 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de

enzyme: thermospermine synthase


organism: Arabidopsis thaliana

substrate_name: pNPP (at pH 7.5 and 30 degrees Celsius)

proof_lines: Experiments have been done in the presence of 100 uM arachidonic acid (AA).

substrate: pNPP (at pH 7.5 and 30 degrees Celsius)


organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)

substrate_name: p-nitrophenylphosphate (at 30 degrees Celsius and at pH 7)

assay_conditions_summary: pH 7

proof_lines: kcat is 5.4 sec(-1) with p-nitrophenylphosphate as substrate (at 30 degrees Celsius and at pH 7).


organism: Escherichia coli (strain K12)

substrate_name: pNPP

proof_lines: kcat is 0.093 sec(-1) with pNPP as substrate.

substrate: pNPP


proof_lines: kcat is 1.52 sec(-1) for the dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 1.25 sec(-1) for the dephosphorylation of pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 0.45 sec(-1)


substrate_name: para-nitrophenylphosphate (at pH 5.5)

proof_lines: kcat is 0.330 sec(-1) for para-nitrophenylphosphate.

substrate: para-nitrophenylphosphate (at pH 5.5)


substrate_name: BCKDHA

proof_lines: kcat is 17.2 min(-1) for BCKDHA. kcat is 43.2 sec(-1) for p-nitrophenylphosphate.

substrate: BCKDHA


substrate_name: pyridoxal 5'-phosphate

proof_lines: kcat varies between 1.5 and 2.0 sec(-1) for the dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 22 degrees Celsius).

substrate: pyridoxal 5'-phosphate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: P-tyr

proof_lines: kcat is 60.0 sec(-1) with P-Tyr as substrate. kcat is 18.32 sec(-1) with P-Ser as substrate. kcat is 12.5 sec(-1) with P-Thr as substrate. kcat is 159.57 sec(-1) with P-Tyr insulin as substrate. kcat is 158.31 sec(-1) with P-Tyr EGFR as sub

substrate: P-tyr


proof_lines: kcat is 14.2 min(-1) for pNPP hydrolysis.


enzyme_display_name: polynucleotide adenylyltransferase

organism: Bos taurus

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature R225Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.3; 310.15 K; cofactor ATP

enzyme: polynucleotide adenylyltransferase

substrate: ATP


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

sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature L213K to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 L213K


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature W230A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature H212A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature N216A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature D218A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 D218A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature R172G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 R172G


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature E209A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 N216A


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature R104A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature Y103G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature F220S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 F220S


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature L105A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature I217T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 direct REST/FASTA lookup on 2026-06-16 and applied mutation signature F220R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 F220R


enzyme_display_name: fumigaclavine B O-acetyltransferase

organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: fumigaclavine B

assay_conditions_summary: cofactor CoA

enzyme: fumigaclavine B O-acetyltransferase

substrate: fumigaclavine B


substrate_name: pNPP (at pH 7.8 and 25 degrees Celsius)

substrate: pNPP (at pH 7.8 and 25 degrees Celsius)


substrate_name: p-nitrophenol phosphate (at pH 6.0)

assay_conditions_summary: pH 6

substrate: p-nitrophenol phosphate (at pH 6.0)


substrate_name: CSNK1E (at 30 degrees Celsius)

substrate: CSNK1E (at 30 degrees Celsius)


substrate_name: p-nitrophenylphosphate


substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature D63A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant D63A
pH 5.0, 20°C, mutant D63A


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature Q136A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant Q136A
pH 5.0, 20°C, mutant Q136A


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature E132L to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant E132L
pH 5.0, 20°C, mutant E132L


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature D63N/E132A 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/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature D63N to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant D63N
pH 5.0, 20°C, mutant D63N


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature R124A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant R124A
pH 5.0, 20°C, mutant R124A


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProt REST/FASTA direct accession check

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

proof_lines:
Raw SKiD Env: Temp=60°C, pH=5
Raw SKiD Env: Temp=20°C, pH=5

source: skid


enzyme_display_name: nicotinamidase

organism: Oceanobacillus iheyensis

substrate_name: Pyrazinamide

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature E65H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; buffer 100 mM phosphate; cofactor NADPH

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block E65H, substrate row PZA; column Specific activity (U/mg) = 0.70±0.03; column Km (mM) = 0.82; column k cat (s-1) = 0.43; column k cat/Km (mM-1 s-1) = 0.52. captured primary segment: PZA | E65H OiNIC | Km 0.82 mM | kcat 0.43 s^-1 | kcat/Km 0.52 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.82 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.82 mM. kcat: printed Table 1 k cat cell 0.43 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.43 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.52 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.52 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.43 / 0.82 = 0.524390243902439 s^-1 mM^-1, against the printed efficiency cell 0.52 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block E65H, substrate row PZA: Km = 0.82 mM; k cat = 0.43 s^-1; k cat/Km = 0.52 mM^-1 s^-1; Specific activity = 0.70±0.03 U/mg.

enzyme: nicotinamidase

substrate: Pyrazinamide

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 displayed sequence; mutation L213K reconstructed from batch signature and applied mutation signature L213K to reconstruct the assayed variant sequence.


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_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation L229R reconstructed from batch signature and applied mutation signature L229R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 L229R


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:P25500 residues 1-513; selected source note names bPAP-513; mutation K228A reconstructed from batch signature and applied mutation signature K228A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 K228A

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant K228A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 displayed sequence; mutation K191A reconstructed from batch signature and applied mutation signature K191A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation W230A reconstructed from batch signature and applied mutation signature W230A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 W230A

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 residues 1-513; selected source note names bPAP-513; mutation T177M reconstructed from batch signature and applied mutation signature T177M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 T177M

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_variant_note: Resolved canonical sequence from UniProtKB:P25500 displayed sequence; mutation S102A reconstructed from batch signature and applied mutation signature S102A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 displayed sequence; mutation L193M reconstructed from batch signature and applied mutation signature L193M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation L105A reconstructed from batch signature and applied mutation signature L105A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 L105A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation D208A reconstructed from batch signature and applied mutation signature D208A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 D208A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation Y103G reconstructed from batch signature and applied mutation signature Y103G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 Y103G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation S102A reconstructed from batch signature and applied mutation signature S102A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 S102A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation Y237A reconstructed from batch signature and applied mutation signature Y237A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 Y237A

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant Y237A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation R225Y reconstructed from batch signature and applied mutation signature R225Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 R225Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 residues 1-513; selected source note names bPAP-513; mutation I217T reconstructed from batch signature and applied mutation signature I217T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 I217T


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25500 displayed sequence; mutation G203H reconstructed from batch signature and applied mutation signature G203H to reconstruct the assayed variant sequence.


organism: Unknown

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


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


organism: Homo sapiens


substrate_name: ATP; UTP

substrate: ATP; UTP


organism: Semliki forest virus

substrate_name: nsP2 RNA triphosphatase activity (at pH 8.0); nsP2 NTPase activity (at pH 7.5)

assay_conditions_summary: pH 8


organism: Venezuelan equine encephalitis virus (strain 3880)

substrate_name: a 12 residues substrate for nsp2 protease activity


organism: Venezuelan equine encephalitis virus (strain Trinidad donkey)

substrate: a 12 residues substrate for nsp2 protease activity


enzyme_display_name: phosphite dehydrogenase

organism: Pseudomonas stutzeri

substrate_name: NAD+; H2O; Phosphonate

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature K76A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant Lys76Ala (N-terminal His6 tag)

enzyme: phosphite dehydrogenase

substrate: NAD+; H2O; Phosphonate


substrate_name: Phosphonate; H2O; NAD+

sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature K76C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant Lys76Cys (N-terminal His6 tag)

substrate: Phosphonate; H2O; NAD+


sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature R237K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant Arg237Lys (N-terminal His6 tag)


substrate_name: H2O; NAD+; Phosphonate

sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature K76M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant Lys76Met (N-terminal His6 tag)

substrate: H2O; NAD+; Phosphonate


substrate_name: phosphonate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature S295A to reconstruct the assayed variant sequence.

smiles: O=[PH](O)O

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADH

column_label: Table 2 (Steady State Parameters of 17X-PTDH Mutants), enzyme-form row 'S295A'; column 'kcat (s-1)' = 2.53; column 'Km,PT (mM)' = 0.103; column 'Km,NAD (mM)' = 0.250; column 'Kia,NAD (mM)' = nd; column 'kcat/Km,PT (M-1 s-1)' = 2.46 x 10^4; column 'Dkcat' = nd; column 'D(kcat/Km,PT)' = nd.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.53 s^-1; already in s^-1, no conversion; the paper value is 2.53 s^(-1). Km: printed Table 2 K_m,PT cell 0.103 mM; already in mM, no conversion; the paper value is 0.103 mM. kcat/Km: printed Table 2 K_cat/K_m,PT cell 2.46 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 24600 / 1000 = 24.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme-form row 'S295A': k_cat = 2.53 s^-1 (column 'kcat (s-1)'); K_m,PT = 0.103 mM (column 'Km,PT (mM)'); printed k_cat/K_m,PT = 2.46 x 10^4 M^-1 s^-1 (column 'kcat/Km,PT (M-1 s-1)').

row_label: Table 2, enzyme-form row 'S295A'

table_label: Table 2: Steady State Parameters of 17X-PTDH Mutants (Biochemistry 2012, 51(21):4254-4262)

substrate: phosphonate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature R301K to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady State Parameters of 17X-PTDH Mutants), enzyme-form row 'R301K'; column 'kcat (s-1)' = 4.50; column 'Km,PT (mM)' = 1.11; column 'Km,NAD (mM)' = 0.074; column 'Kia,NAD (mM)' = 0.97; column 'kcat/Km,PT (M-1 s-1)' = 4050; column 'Dkcat' = 1.90; column 'D(kcat/Km,PT)' = 2.19.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.50 s^-1; already in s^-1, no conversion; the paper value is 4.5 s^(-1). Km: printed Table 2 K_m,PT cell 1.11 mM; already in mM, no conversion; the paper value is 1.11 mM. kcat/Km: printed Table 2 K_cat/K_m,PT cell 4050 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4050 / 1000 = 4.05 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme-form row 'R301K': k_cat = 4.50 s^-1 (column 'kcat (s-1)'); K_m,PT = 1.11 mM (column 'Km,PT (mM)'); printed k_cat/K_m,PT = 4050 M^-1 s^-1 (column 'kcat/Km,PT (M-1 s-1)').

row_label: Table 2, enzyme-form row 'R301K'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature Y139F to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady State Parameters of 17X-PTDH Mutants), enzyme-form row 'Y139F'; column 'kcat (s-1)' = 3.68; column 'Km,PT (mM)' = 0.039; column 'Km,NAD (mM)' = 0.036; column 'Kia,NAD (mM)' = nd; column 'kcat/Km,PT (M-1 s-1)' = 9.44 x 10^4; column 'Dkcat' = nd; column 'D(kcat/Km,PT)' = nd.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.68 s^-1; already in s^-1, no conversion; the paper value is 3.68 s^(-1). Km: printed Table 2 K_m,PT cell 0.039 mM; already in mM, no conversion; the paper value is 0.039 mM. kcat/Km: printed Table 2 K_cat/K_m,PT cell 9.44 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 94400 / 1000 = 94.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme-form row 'Y139F': k_cat = 3.68 s^-1 (column 'kcat (s-1)'); K_m,PT = 0.039 mM (column 'Km,PT (mM)'); printed k_cat/K_m,PT = 9.44 x 10^4 M^-1 s^-1 (column 'kcat/Km,PT (M-1 s-1)').

row_label: Table 2, enzyme-form row 'Y139F'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature W134A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady State Parameters of 17X-PTDH Mutants), enzyme-form row 'W134A'; column 'kcat (s-1)' = 1.73; column 'Km,PT (mM)' = 1.91; column 'Km,NAD (mM)' = 0.187; column 'Kia,NAD (mM)' = nd; column 'kcat/Km,PT (M-1 s-1)' = 901; column 'Dkcat' = 2.16; column 'D(kcat/Km,PT)' = 2.09.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.73 s^-1; already in s^-1, no conversion; the paper value is 1.73 s^(-1). Km: printed Table 2 K_m,PT cell 1.91 mM; already in mM, no conversion; the paper value is 1.91 mM. kcat/Km: printed Table 2 K_cat/K_m,PT cell 901 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 901 / 1000 = 0.901 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme-form row 'W134A': k_cat = 1.73 s^-1 (column 'kcat (s-1)'); K_m,PT = 1.91 mM (column 'Km,PT (mM)'); printed k_cat/K_m,PT = 901 M^-1 s^-1 (column 'kcat/Km,PT (M-1 s-1)').

row_label: Table 2, enzyme-form row 'W134A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature W134F to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady State Parameters of 17X-PTDH Mutants), enzyme-form row 'W134F'; column 'kcat (s-1)' = 2.96; column 'Km,PT (mM)' = 0.238; column 'Km,NAD (mM)' = 0.102; column 'Kia,NAD (mM)' = nd; column 'kcat/Km,PT (M-1 s-1)' = 1.24 x 10^4; column 'Dkcat' = 2.22; column 'D(kcat/Km,PT)' = 2.68.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.96 s^-1; already in s^-1, no conversion; the paper value is 2.96 s^(-1). Km: printed Table 2 K_m,PT cell 0.238 mM; already in mM, no conversion; the paper value is 0.238 mM. kcat/Km: printed Table 2 K_cat/K_m,PT cell 1.24 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12400 / 1000 = 12.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme-form row 'W134F': k_cat = 2.96 s^-1 (column 'kcat (s-1)'); K_m,PT = 0.238 mM (column 'Km,PT (mM)'); printed k_cat/K_m,PT = 1.24 x 10^4 M^-1 s^-1 (column 'kcat/Km,PT (M-1 s-1)').

row_label: Table 2, enzyme-form row 'W134F'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature R301A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady State Parameters of 17X-PTDH Mutants), enzyme-form row 'R301A'; column 'kcat (s-1)' = 0.041; column 'Km,PT (mM)' = 19.4; column 'Km,NAD (mM)' = 0.216; column 'Kia,NAD (mM)' = 0.48; column 'kcat/Km,PT (M-1 s-1)' = 2.11; column 'Dkcat' = 2.7; column 'D(kcat/Km,PT)' = 2.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.041 s^-1; already in s^-1, no conversion; the paper value is 0.041 s^(-1). Km: printed Table 2 K_m,PT cell 19.4 mM; already in mM, no conversion; the paper value is 19.4 mM. kcat/Km: printed Table 2 K_cat/K_m,PT cell 2.11 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.11 / 1000 = 0.00211 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme-form row 'R301A': k_cat = 0.041 s^-1 (column 'kcat (s-1)'); K_m,PT = 19.4 mM (column 'Km,PT (mM)'); printed k_cat/K_m,PT = 2.11 M^-1 s^-1 (column 'kcat/Km,PT (M-1 s-1)').

row_label: Table 2, enzyme-form row 'R301A'


sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature E175A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature M53N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O69054 FASTA plus direct residue-coordinate check and applied mutation signature M53A to reconstruct the assayed variant sequence.


organism: Ralstonia sp.

substrate_name: NAD+

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

sequence_source: UniProt G4XDR8 FASTA

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

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NAD+

proof_lines:
pH 7.2, 30°C
pH 7.2, 40°C
Raw SKiD Env: Temp=30°C, pH=7.2

source_databases_merged: brenda skid

substrate: NAD+


organism: Ralstonia sp. 4506

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


sequence_variant_note: Resolved canonical sequence from UniProt G4XDR8 FASTA plus direct residue-coordinate check and applied mutation signature Y139F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature Y139W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature Y139R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature Y139L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature Y139M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature Y139Q to reconstruct the assayed variant sequence.


organism: Stutzerimonas stutzeri

substrate_name: phosphite

sequence_source: UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows

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

substrate: phosphite


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

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NAD+

proof_lines:
Opt14 variant
mutant 17X-PTDH, pH 7.3, 25°C
Opt12 and Opt13 variants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature R301K to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature S295A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature M53A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup; residue-coordinate reconstruction for substitution rows and applied mutation signature E175A to reconstruct the assayed variant sequence.


substrate_name: H2O; Phosphonate; NAD+

sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence reconstructed with selected-batch mutation_signature E175A and applied mutation signature E175A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant E175A

substrate: H2O; Phosphonate; NAD+


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence reconstructed with selected-batch mutation_signature E175A/A176R and applied mutation signature E175A/A176R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant E175A, A176R


sequence_source: UniProtKB O69054 canonical sequence from direct REST/FASTA lookup on 2026-06-16


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature E175A/A176R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.25; 298.15 K; cofactor NADP+

column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'E175A, A176R'; column 'KM (µM, NADP+)' = 3.5; column 'kcat (min-1)' (the NADP+ block) = 114.0; column 'kcat/KM,NADP (µM-1 min-1)' = 32.6. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NAD+ block.

raw_value_unit_evidence: Table 1, enzyme row 'E175A, A176R', NADP+ block: KM = 3.5 uM; kcat = 114.0 min^-1; kcat/KM = 32.6 uM^-1 min^-1.

row_label: Table 1, enzyme row 'E175A, A176R', the three NADP+ cells (KM for NADP+, kcat, kcat/KM)

substrate: NADP+


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

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.3
Raw SKiD Env: Temp=-----, pH=-----


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature E175A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'E175A'; column 'KM (µM, NADP+)' = 144; column 'kcat (min-1)' (the NADP+ block) = 130.8; column 'kcat/KM,NADP (µM-1 min-1)' = 0.91. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NAD+ block.

raw_value_unit_evidence: Table 1, enzyme row 'E175A', NADP+ block: KM = 144 uM; kcat = 130.8 min^-1; kcat/KM = 0.91 uM^-1 min^-1.

row_label: Table 1, enzyme row 'E175A', the three NADP+ cells (KM for NADP+, kcat, kcat/KM)

status: verified


substrate_name: Phosphonate; NAD+; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical sequence reconstructed with selected-batch mutation_signature A176R and applied mutation signature A176R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant A176R

substrate: Phosphonate; NAD+; H2O


column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'WT'; column 'KM (µM, NADP+)' = 2510; column 'kcat (min-1)' (the NADP+ block) = 84.6; column 'kcat/KM,NADP (µM-1 min-1)' = 0.0337. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NAD+ block.

raw_value_unit_evidence: Table 1, enzyme row 'WT', NADP+ block: KM = 2510 uM; kcat = 84.6 min^-1; kcat/KM = 0.0337 uM^-1 min^-1.

row_label: Table 1, enzyme row 'WT', the three NADP+ cells (KM for NADP+, kcat, kcat/KM)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O69054 and applied mutation signature A176R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.25; 298.15 K; cofactor NAD+

column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'A176R'; column 'KM (µM, NAD+)' = 60; column 'kcat (min-1)' (the NAD+ block) = 256.8; column 'kcat/KM,NAD (µM-1 min-1)' = 4.3. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NADP+ block.

raw_value_unit_evidence: Table 1, enzyme row 'A176R', NAD+ block: KM = 60 uM; kcat = 256.8 min^-1; kcat/KM = 4.3 uM^-1 min^-1.

row_label: Table 1, enzyme row 'A176R', the three NAD+ cells (KM for NAD+, kcat, kcat/KM)


column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'E175A'; column 'KM (µM, NAD+)' = 16; column 'kcat (min-1)' (the NAD+ block) = 210.0; column 'kcat/KM,NAD (µM-1 min-1)' = 13.1. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NADP+ block.

raw_value_unit_evidence: Table 1, enzyme row 'E175A', NAD+ block: KM = 16 uM; kcat = 210.0 min^-1; kcat/KM = 13.1 uM^-1 min^-1.

row_label: Table 1, enzyme row 'E175A', the three NAD+ cells (KM for NAD+, kcat, kcat/KM)


column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'A176R'; column 'KM (µM, NADP+)' = 77; column 'kcat (min-1)' (the NADP+ block) = 130.8; column 'kcat/KM,NADP (µM-1 min-1)' = 1.7. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NAD+ block.

raw_value_unit_evidence: Table 1, enzyme row 'A176R', NADP+ block: KM = 77 uM; kcat = 130.8 min^-1; kcat/KM = 1.7 uM^-1 min^-1.

row_label: Table 1, enzyme row 'A176R', the three NADP+ cells (KM for NADP+, kcat, kcat/KM)


column_label: Table 1: Kinetic Parameters for Recombinant WT Phosphite Dehydrogenase and Mutants Using NADP+ and NAD+ as Substrates (Biochemistry 2003, 42, 11604-11614); enzyme row 'E175A, A176R'; column 'KM (µM, NAD+)' = 20; column 'kcat (min-1)' (the NAD+ block) = 236.4; column 'kcat/KM,NAD (µM-1 min-1)' = 11.8. The KM (µM, Pt-H) cell of the same block is the phosphite Michaelis constant, and the remaining four cells of the printed row belong to the NADP+ block.

raw_value_unit_evidence: Table 1, enzyme row 'E175A, A176R', NAD+ block: KM = 20 uM; kcat = 236.4 min^-1; kcat/KM = 11.8 uM^-1 min^-1.

row_label: Table 1, enzyme row 'E175A, A176R', the three NAD+ cells (KM for NAD+, kcat, kcat/KM)


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: phosphonate dehydrogenase(Enzyme) mutant Glu266Gln (N-terminal His6 tag)


proof_lines: SABIO-RK modifier species: phosphonate dehydrogenase(Enzyme) mutant Lys76Arg (N-terminal His6 tag)


enzyme_display_name: thymidine phosphorylase

organism: Escherichia coli

sequence_source: UniProtKB P07650 / TYPH_ECOLI, Escherichia coli K12 thymidine phosphorylase, EC 2.4.2.4; direct UniProt REST accession check on 2026-06-16

assay_conditions_summary: pH 6.5; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 6.5), at 25°C

proof_lines: in 50 mM potassium phosphate buffer, pH 6.5, 25°C

enzyme: thymidine phosphorylase


substrate_name: thymidine

substrate: thymidine


substrate_name: Unknown

ki_unit: mM

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

proof_lines: pH not specified in the publication, 30°C

substrate: Unknown


substrate_name: thymine

substrate: thymine


sequence_source: UniProtKB P19971 / TYPH_HUMAN, Homo sapiens thymidine phosphorylase, EC 2.4.2.4; direct UniProt REST accession check on 2026-06-16

proof_lines: ph 5.5, 37°C, recombinant wild-type enzyme


substrate_name: Phosphate; Uridine

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

assay_conditions_summary: pH 7.5; 310.15 K; buffer 0.1 M potassium phosphate

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

source_databases_merged: sabio_rk brenda skid

substrate: Phosphate; Uridine


organism: Mus musculus

sequence_source: UniProtKB Q99N42 / TYPH_MOUSE, Mus musculus thymidine phosphorylase, EC 2.4.2.4; direct UniProt REST accession check on 2026-06-16


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

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 F220Y


mutation_type: deletion

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) wildtype bPAP-513 (C-terminal deletion)


substrate_name: ATP

substrate: ATP


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 F243A

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


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 L193M


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))

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 R221A


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 R104A

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))


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 K191A


proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 G203H

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant G203H


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 F220R 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 L229R 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 R225N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 R225N


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 F243A 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 L211K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: polynucleotide adenylyltransferase(Enzyme) mutant bPAP-513 L211K


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


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.


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.


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

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

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

substrate_name: UDP-D-glucosamine

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

enzyme: hyaluronan synthase

substrate: UDP-D-glucosamine


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


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


organism: Bos taurus

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


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

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.

substrate: ATP


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


organism: Homo sapiens

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

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


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

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=-----

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.

assay_conditions_summary: pH 8.3; 310.15 K; cofactor ATP


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.

assay_conditions_summary: cofactor ATP

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


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_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


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

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 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)


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

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.

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.


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)


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


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.


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.


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