sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q46893 and applied mutation signature R20A to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-State Kinetic Parameters for E. coli wt YgbP and Mutants (Biochemistry 2004, volume 43, number 38, pages 12189-12197). The table is printed as two halves. The MEP half carries the column heads Km (mM), appkcat (s-1), Calckcat (s-1) and kcat/Km (s-1 mM-1); the CTP half carries Km (mM), Ki (mM), Obskcat (s-1) and kcat/Km (s-1 mM-1). This record reads the enzyme row R20A along its MEP half: column Km (mM) = 3.28; column Calckcat (s-1) = 52.7; column kcat/Km (s-1 mM-1) = 16.

normalized_value_unit_evidence: kcat: printed cell 52.7 in the column Calckcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 52.7 s^(-1). Km: printed cell 3.28 in the column Km (mM); mM is already canonical, so no unit conversion applies and the value is 3.28 mM. kcat/Km: the MEP half of this line prints the catalytic-efficiency cell 16 s-1 mM-1; 1 s-1 mM-1 is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 16.0 s^(-1)*mM^(-1). This catalog row carries no kcat_over_km field, so that printed cell is recorded as typed provenance only and no efficiency value is proposed.

raw_value_unit_evidence: Table 1, enzyme row R20A, MEP half: Km = 3.28 mM; Calckcat = 52.7 s-1; printed kcat/Km = 16 s-1 mM-1.

row_label: Table 1, enzyme row R20A, MEP half (MEP as the varied substrate)


organism: Escherichia coli

kcat_over_km_display: Not reported

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

km_unit: mM

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProt Q46893 with T140V reconstructed from canonical residue T140 and applied mutation signature T140V to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant T140V


sequence_variant_note: Resolved canonical sequence from UniProt Q46893 with R20A reconstructed from canonical residue R20 and applied mutation signature R20A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant R20A


substrate_name: 2-C-Methyl-D-erythritol 4-phosphate

source_db: oed

verification_status: verified

ki_display: Not reported

kcat_over_km_origin: calculated

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q46893 and applied mutation signature R19K to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-State Kinetic Parameters for E. coli wt YgbP and Mutants (Biochemistry 2004, volume 43, number 38, pages 12189-12197). The table is printed as two halves. The MEP half carries the column heads Km (mM), appkcat (s-1), Calckcat (s-1) and kcat/Km (s-1 mM-1); the CTP half carries Km (mM), Ki (mM), Obskcat (s-1) and kcat/Km (s-1 mM-1). This record reads the enzyme row R19K along its MEP half: column Km (mM) = 0.74; column Calckcat (s-1) = 47.2; column kcat/Km (s-1 mM-1) = 64.

normalized_value_unit_evidence: kcat: printed cell 47.2 in the column Calckcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 47.2 s^(-1). Km: printed cell 0.74 in the column Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.74 mM. kcat/Km: the MEP half of this line prints the catalytic-efficiency cell 64 s-1 mM-1; 1 s-1 mM-1 is already the canonical s^(-1)*mM^(-1), so no unit conversion applies. The exact quotient of the two printed component cells of the same line is 47.2 / 0.74 = 63.78378378378379 s^(-1)*mM^(-1), and the printed cell is that same quotient carried to the precision the table prints.

raw_value_unit_evidence: Table 1, enzyme row R19K, MEP half: Km = 0.74 mM; Calckcat = 47.2 s-1; printed kcat/Km = 64 s-1 mM-1.

row_label: Table 1, enzyme row R19K, MEP half (MEP as the varied substrate)

data_origin: experimental

substrate: 2-C-Methyl-D-erythritol 4-phosphate

status: verified

source: oed


substrate_name: CTP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q46893 and applied mutation signature R20K to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-State Kinetic Parameters for E. coli wt YgbP and Mutants (Biochemistry 2004, volume 43, number 38, pages 12189-12197). The table is printed as two halves. The MEP half carries the column heads Km (mM), appkcat (s-1), Calckcat (s-1) and kcat/Km (s-1 mM-1); the CTP half carries Km (mM), Ki (mM), Obskcat (s-1) and kcat/Km (s-1 mM-1). This record reads the enzyme row R20K along its CTP half: column Km (mM) = 3.7; column Obskcat (s-1) = 53.6; column kcat/Km (s-1 mM-1) = 14.5.

normalized_value_unit_evidence: kcat: printed cell 53.6 in the column Obskcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 53.6 s^(-1). Km: printed cell 3.7 in the column Km (mM); mM is already canonical, so no unit conversion applies and the value is 3.7 mM. kcat/Km: the CTP half of this line prints the catalytic-efficiency cell 14.5 s-1 mM-1; 1 s-1 mM-1 is already the canonical s^(-1)*mM^(-1), so no unit conversion applies. The exact quotient of the two printed component cells of the same line is 53.6 / 3.7 = 14.486486486486486 s^(-1)*mM^(-1), and the printed cell is that same quotient carried to the precision the table prints.

raw_value_unit_evidence: Table 1, enzyme row R20K, CTP half: Km = 3.7 mM; Obskcat = 53.6 s-1; printed kcat/Km = 14.5 s-1 mM-1.

row_label: Table 1, enzyme row R20K, CTP half (CTP as the varied substrate)

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProt Q46893 with K27S reconstructed from canonical residue K27 and applied mutation signature K27S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant K27S


sequence_variant_note: Resolved canonical sequence from UniProt Q46893 with R19A reconstructed from canonical residue R19 and applied mutation signature R19A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant R19A


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


mutation_signature: Unknown

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


substrate_name: 2-C-methyl-D-erythritol 4-phosphate

verification_status: unverified

protein_accession_database: UniProt

sequence_source: UniProtKB Q46893 direct lookup, accessed 2026-06-10

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

substrate: 2-C-methyl-D-erythritol 4-phosphate

status: unverified


organism: Mycobacterium tuberculosis

source_db: brenda

kcat_display: Not reported

sequence_source: UniProtKB P9WKG9 direct lookup, accessed 2026-06-10

source: brenda


organism: Plasmodium falciparum

sequence_source: UniProtKB Q8I273 direct lookup, accessed 2026-06-10


organism: Plasmodium vivax

sequence_source: UniProtKB REST FASTA accession A5K9U5


enzyme_display_name: cephalosporin-C deacetylase

organism: Bacillus subtilis

substrate_name: 7-Aminocephalosporanic acid; H2O

sequence_source: UniProtKB REST FASTA accession P94388

enzyme: cephalosporin-C deacetylase

substrate: 7-Aminocephalosporanic acid; H2O


sequence_source: UniProtKB REST FASTA accession M1JUH6

proof_lines:
immobilized enzyme, pH 6.5, 25°C
free enzyme, pH 6.5, 25°C


organism: Thermotoga maritima

substrate_name: fluorescein divaleryloxymethyl ether

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

sequence_source: UniProtKB REST FASTA accession Q9WXT2

proof_lines:
pH 7.3, 25°C
Raw SKiD Env: Temp=50°C, pH=8
Raw SKiD Env: Temp=25°C, pH=7.3

source_databases_merged: brenda skid

substrate: fluorescein divaleryloxymethyl ether


substrate_name: 7-aminocephalosporanic acid

proof_lines: wild-type including expression and purification tag, pH 8.0, 50°C

substrate: 7-aminocephalosporanic acid


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

proof_lines: mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C

proof_lines: mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C


substrate_name: 7-Aminocephalosporanic acid

substrate: 7-Aminocephalosporanic acid


substrate_name: Glucose pentaacetate

substrate: Glucose pentaacetate


enzyme_display_name: phospholipase D

organism: Streptomyces antibioticus

substrate_name: dioleoyl-phosphatidylcholine

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:Q53728 direct accession lookup 2026-06-10

enzyme: phospholipase D

substrate: dioleoyl-phosphatidylcholine

source: skid


organism: Streptomyces chromofuscus

substrate_name: H2O; 4-Nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KRU5 direct accession lookup 2026-06-10 and applied mutation signature D389A with inferred residue-numbering offset +46 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase D(Enzyme) mutant D389A

substrate: H2O; 4-Nitrophenyl phosphate


substrate_name: 4-Nitrophenyl phosphocholine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KRU5 direct accession lookup 2026-06-10 and applied mutation signature H212A with inferred residue-numbering offset +46 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase D(Enzyme) mutant H212A

substrate: 4-Nitrophenyl phosphocholine; H2O


substrate_name: H2O; 4-Nitrophenyl phosphocholine

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

sequence_source: UniProtKB:Q8KRU5 direct accession lookup 2026-06-10

substrate: H2O; 4-Nitrophenyl phosphocholine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KRU5 direct accession lookup 2026-06-10 and applied mutation signature E213A with inferred residue-numbering offset +46 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase D(Enzyme) mutant E213A


organism: Streptomyces cinnamoneus

substrate_name: yolk phosphatidylcholine

substrate: yolk phosphatidylcholine


organism: Streptomyces sp. NA684


substrate_name: L-alpha-lysophosphatidylcholine

substrate: L-alpha-lysophosphatidylcholine


organism: Thermocrispum sp.


proof_lines: SABIO-RK modifier species: phospholipase D(Enzyme) mutant F211A C-terminal His6-tag


enzyme_display_name: beta-amylase

organism: Bacillus cereus

substrate_name: amylose

sequence_variant_note: Mutation signature S235A/Y249A matches the mutant residue at offset +30 and the reference residue at offset -24; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 7, 25°C, DPn: 16, S235A/Y249A double mutant

proof_lines: pH 7, 25°C, S235A/Y249A double mutant, amylose as substrate

enzyme: beta-amylase

substrate: amylose


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature W449F/W495F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: pH 7, 25°C, DPn: 16, W449F/W495F double mutant


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature S235A/Y249A/W449F/W495F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: pH 7, 25°C, DPn: 16, S235A/Y249A/W449F/W495F quadruple mutant

proof_lines: pH 7, 25°C, S235A/Y249A/W449F/W495F quadruple mutant, amylose as substrate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Y249A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S235A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: amylopectin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P36924 canonical sequence; mutation reconstructed with mature-enzyme numbering offset +30 from UniProt Signal 1-30/Chain 31-546 and applied mutation signature Y164H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

substrate: amylopectin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P36924 canonical sequence; mutation reconstructed with mature-enzyme numbering offset +30 from UniProt Signal 1-30/Chain 31-546 and applied mutation signature Y164E with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P36924 canonical sequence, direct UniProt REST/FASTA check on 2026-06-10

proof_lines: pH 7, 25°C, wild-type enzyme, amylose as substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P36924 canonical sequence; mutation reconstructed with mature-enzyme numbering offset +30 from UniProt Signal 1-30/Chain 31-546 and applied mutation signature Y164Q with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P36924 canonical sequence; mutation reconstructed with mature-enzyme numbering offset +30 from UniProt Signal 1-30/Chain 31-546 and applied mutation signature T47M/Y164E/T328N with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: 37°C, recombinant mutant T47M/Y164E/T328N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P36924 canonical sequence; mutation reconstructed with mature-enzyme numbering offset +30 from UniProt Signal 1-30/Chain 31-546 and applied mutation signature Y164F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


substrate_name: Maltopentaose; H2O

substrate: Maltopentaose; H2O


proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


substrate_name: 4-nitrophenyl acetate

sequence_source: UniProtKB reviewed accession Q9WXT2 FASTA fetched from rest.uniprot.org on 2026-06-10.

substrate: 4-nitrophenyl acetate


substrate_name: xylose tetraacetate

substrate: xylose tetraacetate


substrate_name: 4-Methylumbelliferyl acetate

substrate: 4-Methylumbelliferyl acetate


organism: Brassica juncea var. juncea

substrate_name: phosphatidylcholine

sequence_source: UniProtKB TrEMBL accession A0A0G4AKV1 FASTA fetched from rest.uniprot.org on 2026-06-10.

substrate: phosphatidylcholine


organism: Moritella sp. JT01

substrate_name: L-alpha-phosphatidylcholine

substrate: L-alpha-phosphatidylcholine


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

proof_lines: pH 8.0, 35°C, mutant enzyme S148C/T206C/D225C/A328C


proof_lines: mutant W187F/Y191R, Vmax: 1.8 micromol/min/mg


sequence_source: UniProtKB reviewed accession Q53728 FASTA fetched from rest.uniprot.org on 2026-06-10.


enzyme_display_name: 2-aminoadipate transaminase

organism: Thermus thermophilus

sequence_source: UniProtKB Q72LL6 direct accession lookup; reviewed Swiss-Prot entry fetched 2026-06-10.

enzyme: 2-aminoadipate transaminase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72LL6 direct accession lookup; S20E reconstructed from canonical sequence fetched 2026-06-10. and applied mutation signature S20E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72LL6 direct accession lookup; R23Q reconstructed from canonical sequence fetched 2026-06-10. and applied mutation signature R23Q to reconstruct the assayed variant sequence.


substrate_name: L-2-Aminoadipate; 2-Oxoglutarate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q72LL6 direct accession lookup; R23A reconstructed from canonical sequence fetched 2026-06-10. and applied mutation signature R23A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 318.15 K; buffer 50 mM HEPES-NaOH

proof_lines: SABIO-RK modifier species: 2-aminoadipate transaminase(Enzyme) mutant R23A

proof_lines: mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5-phosphate, at 45°C

proof_lines: mutant enzyme R23A, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5-phosphate, at 45°C

substrate: L-2-Aminoadipate; 2-Oxoglutarate


substrate_name: L-leucine

sequence_source: UniProtKB Q72LL6 direct accession lookup; R23A reconstructed from canonical sequence fetched 2026-06-10.

substrate: L-leucine


substrate_name: L-glutamate

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

substrate: L-glutamate


substrate_name: 2-Oxoglutarate; L-2-Aminoadipate

sequence_source: UniProtKB Q72LL6 direct accession lookup; R23Q reconstructed from canonical sequence fetched 2026-06-10.

proof_lines: SABIO-RK modifier species: 2-aminoadipate transaminase(Enzyme) mutant R23Q

proof_lines: mutant enzyme R23Q, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5-phosphate, at 45°C

proof_lines: mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5-phosphate, at 45°C

substrate: 2-Oxoglutarate; L-2-Aminoadipate


organism: Calystegia sepium

substrate_name: Unknown

km_display: Not reported

sequence_source: UniProtKB Q9FQ07 FASTA/JSON direct accession lookup

substrate: Unknown


organism: Glycine max

substrate_name: maltopentaose

sequence_source: UniProtKB P10538 FASTA/JSON direct accession lookup

proof_lines: pH 5.4, 37°C, recombinant wild-type enzyme

substrate: maltopentaose


sequence_source: Reconstructed from UniProtKB P10538 canonical sequence using PMID 15178253 and UniProt mutagenesis-position offset

sequence_variant_note: Mutation signature E186Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P10538 canonical sequence using PMID 15178253 and UniProt mutagenesis-position offset and applied mutation signature E380Q with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P10538 canonical sequence using PMID 15794648 and UniProt crystallography-position offset and applied mutation signature T342A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P10538 canonical sequence using PMID 15794648 and UniProt crystallography-position offset and applied mutation signature T342S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P10538 canonical sequence using PMID 15794648 and UniProt crystallography-position offset and applied mutation signature T342V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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

sequence_source: UniProt Q72LL6 direct accession check


sequence_source: UniProt Q72LL6 canonical sequence checked; row-specific variant not resolved

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


verification_status: corrected

sequence_source: UniProt Q72LL6 reviewed canonical sequence

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProt Q72LL6 canonical sequence with direct R23Q reconstruction and applied mutation signature R23Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q72LL6 canonical sequence with direct S20E reconstruction and applied mutation signature S20E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-aminoadipate transaminase(Enzyme) mutant S20E

proof_lines: mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5-phosphate, at 45°C

proof_lines: mutant enzyme S20E, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5-phosphate, at 45°C


sequence_source: UniProt Q72LL6 canonical sequence with direct S20E reconstruction


proof_lines: wild type enzyme, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5-phosphate, at 45°C

proof_lines: wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5-phosphate, at 45°C

proof_lines: wild type enzyme, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5-phosphate, at 45°C


enzyme_display_name: pullulanase

organism: Anoxybacillus sp. WB42

substrate_name: pullulan

enzyme: pullulanase

substrate: pullulan


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

proof_lines: recombinant wild-type enzyme, pH 6.2, 65°C


sequence_source: UniProtKB:C0SPA0 direct lookup 2026-06-10

proof_lines: calculated by BRENDA, pH 6.0, 45°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:C0SPA0 direct lookup 2026-06-10 plus selected BRENDA mutation signature D465E and applied mutation signature D465E to reconstruct the assayed variant sequence.

proof_lines: calculated by BRENDA, pH 6.0, 45°C, recombinant mutant D465E


sequence_variant_note: Resolved canonical sequence from UniProtKB:C0SPA0 direct lookup 2026-06-10 plus selected BRENDA mutation signature D465N and applied mutation signature D465N to reconstruct the assayed variant sequence.

proof_lines: calculated by BRENDA, pH 6.0, 45°C, recombinant mutant D465N


organism: Enterobacter aerogenes

substrate_name: Pullulan; H2O

sequence_source: UniProtKB:P07811 direct lookup 2026-06-10; canonical sequence retained only as context

proof_lines: SABIO-RK modifier species: pullulanase(Enzyme) mutant I-27

proof_lines: SABIO-RK modifier species: pullulanase(Enzyme) mutant I-35

proof_lines: SABIO-RK modifier species: pullulanase(Enzyme) mutant I-56

substrate: Pullulan; H2O


sequence_source: UniProtKB:P07811 direct lookup 2026-06-10


organism: Exiguobacterium sp.


organism: Pullulanibacillus naganoensis

sequence_source: UniProtKB:G9JLV4 direct lookup 2026-06-10; fragment canonical sequence retained only as context

proof_lines: pH 5.0, 55°C, recombinant mutant PulA-N3 enzyme


km_unit: mg mL^-1

sequence_source: UniProtKB G9JLV4 direct accession check

proof_lines: pH 5.0, 55°C, recombinant wild-type enzyme


organism: Pyrococcus yayanosii

sequence_source: UniProtKB F8AHK0 direct accession check

proof_lines: recombinant wild-type enzyme, pH 5.0, 100°C


sequence_source: UniProtKB F8AHK0 canonical sequence checked; row-specific variant not resolved


proof_lines: recombinant mutant Q13H/I25E, pH 5.0, 100°C


organism: Thermoanaerobacterium saccharolyticum

substrate_name: soluble starch

mutation_signature: truncated enzyme form ApuM957

sequence_source: UniProtKB C5IGQ7 canonical sequence checked; row-specific truncation not resolved

mutation_type: truncation

proof_lines: truncated enzyme form ApuM957, at pH 6.0 and 70°C

proof_lines: truncated enzyme form ApuM957, at pH 5.0 and 70°C

substrate: soluble starch


mutation_signature: truncated enzyme form ApuK855

proof_lines: truncated enzyme form ApuK855, at pH 6.0 and 70°C

proof_lines: truncated enzyme form ApuK855, at pH 5.0 and 70°C


organism: Thermofilum pendens

substrate_name: gamma-cyclodextrin

sequence_source: UniProtKB A1RWP0 direct accession check

substrate: gamma-cyclodextrin


enzyme_display_name: glucan 1,4-beta-glucosidase

organism: Hordeum vulgare

substrate_name: Laminaritetraose

sequence_source: UniProtKB:Q42835 direct REST lookup; live TrEMBL entry Q42835_HORVU; sequence version 1; organism Hordeum vulgare

enzyme: glucan 1,4-beta-glucosidase

substrate: Laminaritetraose


substrate_name: Cellopentaose

substrate: Cellopentaose


substrate_name: Cellobiose

substrate: Cellobiose


substrate_name: Cellotetraose

substrate: Cellotetraose


substrate_name: cellotriose

substrate: cellotriose


substrate_name: Cellobiose; H2O

substrate: Cellobiose; H2O


substrate_name: laminaribiose

substrate: laminaribiose


organism: Thermobifida fusca

substrate_name: 2,4-dinitrophenol cellobiose

substrate: 2,4-dinitrophenol cellobiose


enzyme_display_name: Glycoside hydrolase, family 57

sequence_source: UniProtKB:A1RWP0 direct REST lookup on 2026-06-10

enzyme: Glycoside hydrolase, family 57


substrate_name: alpha-cyclodextrin

substrate: alpha-cyclodextrin


substrate_name: beta-cyclodextrin

substrate: beta-cyclodextrin


enzyme_display_name: Pullulanase-type starch debranching enzyme

organism: Zea mays

sequence_source: UniProtKB:O81638 direct REST lookup on 2026-06-10


enzyme_display_name: Beta-glucosidase

organism: Clostridium cellulovorans

sequence_source: UniProtKB:Q53EH2 direct REST lookup on 2026-06-10

enzyme: Beta-glucosidase


enzyme_display_name: CHU large protein candidate b-glycosidase, glycoside hydrolase family 9 protein

organism: Cytophaga hutchinsonii

substrate_name: 4-nitrophenyl alpha-D-glucoside

sequence_source: UniProtKB:A0A6N4SPK1 direct REST lookup on 2026-06-10

proof_lines: pH 6.5, 35°C, catalytic module of CHU_0961 (CHU_0961B)

substrate: 4-nitrophenyl alpha-D-glucoside


enzyme_display_name: 1,4-beta-D-glucan glucohydrolase

organism: Fibrobacter succinogenes subsp. succinogenes S85

substrate_name: cellohexaose

sequence_source: UniProtKB:B0FWI3 direct REST lookup on 2026-06-10

enzyme: 1,4-beta-D-glucan glucohydrolase

substrate: cellohexaose


enzyme_display_name: Beta-D-glucan exohydrolase, isoenzyme ExoII

sequence_source: UniProtKB:Q42835 direct REST lookup on 2026-06-10


organism: Ipomoea batatas

substrate_name: starch

sequence_source: UniProtKB:P10537 direct lookup, sequence version 4

proof_lines:
immobilized enzyme, pH 7.0, 40°C
free enzyme, pH 7.0, 40°C

substrate: starch


organism: Pyrococcus furiosus

substrate_name: 4-nitrophenyl alpha-maltopyranoside

sequence_source: UniProtKB:Q8U2G5 direct lookup, sequence version 1

substrate: 4-nitrophenyl alpha-maltopyranoside


organism: Thermococcus sp.

substrate_name: maltotetraose

sequence_source: UniProtKB:I3ZTN9 direct lookup, sequence version 1

substrate: maltotetraose


substrate_name: pullulan

substrate: pullulan


proof_lines: recombinant enzyme mutant PulAC, pH 6.6, 65°C


organism: Lactococcus lactis subsp. lactis

substrate_name: o-Nitrophenyl-beta-D-galactoside; H2O

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11546 and applied mutation signature K435V/Y437F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer sodium phosphate

column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row K435V/Y437F, Substrate row ONPG; column kcat (min-1) = 3.81 x 10^-3 ± 3.85 x 10^-4; column Km (mM) = 0.57 ± 0.02; column kcat/Km (min-1 mM-1) = 6.66 x 10^-3 ± 9.38 x 10^-4; column ddG (kJ/mol) = –0.54. captured primary segment: K435V/Y437F | ONPG | kcat 3.81 x 10^-3 min^-1 (± 3.85 x 10^-4) | Km 0.57 mM (± 0.02) | kcat/Km 6.66 x 10^-3 min^-1 mM^-1 (± 9.38 x 10^-4) | ddG(kJ/mol) –0.54

normalized_value_unit_evidence: kcat: printed Table I cell 3.81 x 10^-3 min^-1; 1 min^-1 is 1/60 s^-1, so 3.81 x 10^-3 / 60 = 0.0000635 s^-1; the exported value is 0.0001185 s^(-1). Km: printed Table I cell 0.57 mM; already in mM, no unit conversion applies; the exported value is 0.57 mM. kcat/Km: Printed Table I kcat/Km cell 6.66 x 10^-3 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6.66 x 10^-3 / 60 = 0.000111 s^-1 mM^-1. The live export row stores no kcat_over_km field for this identity. Quotient disclosure for this row: 0.0000635 / 0.57 = 0.00011140350877192984 s^-1 mM^-1, against the printed efficiency cell 0.000111 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Type row K435V/Y437F, Substrate row ONPG: kcat = 3.81 x 10^-3 min^-1 (printed error ± 3.85 x 10^-4); Km = 0.57 mM (printed error ± 0.02); printed kcat/Km = 6.66 x 10^-3 min^-1 mM^-1 (printed error ± 9.38 x 10^-4); ddG = –0.54 kJ/mol.

substrate: o-Nitrophenyl-beta-D-galactoside; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11546 and applied mutation signature W429A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 295.15 K; buffer sodium phosphate

column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row W429A, Substrate row PNPG-6-P; column kcat (min-1) = 2.44 x 10^-4 ± 1.22 x 10^-5; column Km (mM) = 3.10 ± 0.72; column kcat/Km (min-1 mM-1) = 7.87 x 10^-5 ± 2.89 x 10^-6; column ddG (kJ/mol) = –19.36. captured primary segment: W429A | PNPG-6-P | kcat 2.44 x 10^-4 min^-1 (± 1.22 x 10^-5) | Km 3.10 mM (± 0.72) | kcat/Km 7.87 x 10^-5 min^-1 mM^-1 (± 2.89 x 10^-6) | ddG(kJ/mol) –19.36

raw_value_unit_evidence: Table I, Type row W429A, Substrate row PNPG-6-P: kcat = 2.44 x 10^-4 min^-1 (printed error ± 1.22 x 10^-5); Km = 3.10 mM (printed error ± 0.72); printed kcat/Km = 7.87 x 10^-5 min^-1 mM^-1 (printed error ± 2.89 x 10^-6); ddG = –19.36 kJ/mol.


substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

sequence_source: UniProtKB P11546 direct FASTA/JSON check plus selected source accession evidence

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

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row W429A, Substrate row PNPGlc-6-P; column kcat (min-1) = 1.28 x 10^-2 ± 1.47 x 10^-3; column Km (mM) = 21.53 ± 2.49; column kcat/Km (min-1 mM-1) = 5.95 x 10^-4 ± 5.89 x 10^-5; column ddG (kJ/mol) = –7.53. captured primary segment: W429A | PNPGlc-6-P | kcat 1.28 x 10^-2 min^-1 (± 1.47 x 10^-3) | Km 21.53 mM (± 2.49) | kcat/Km 5.95 x 10^-4 min^-1 mM^-1 (± 5.89 x 10^-5) | ddG(kJ/mol) –7.53

raw_value_unit_evidence: Table I, Type row W429A, Substrate row PNPGlc-6-P: kcat = 1.28 x 10^-2 min^-1 (printed error ± 1.47 x 10^-3); Km = 21.53 mM (printed error ± 2.49); printed kcat/Km = 5.95 x 10^-4 min^-1 mM^-1 (printed error ± 5.89 x 10^-5); ddG = –7.53 kJ/mol.


substrate_name: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate

column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row W429A, Substrate row ONPG-6-P; column kcat (min-1) = 1.19 x 10^-3 ± 4.82 x 10^-4; column Km (mM) = 2.86 ± 0.14; column kcat/Km (min-1 mM-1) = 4.16 x 10^-4 ± 2.02 x 10^-5; column ddG (kJ/mol) = –17.08. captured primary segment: W429A | ONPG-6-P | kcat 1.19 x 10^-3 min^-1 (± 4.82 x 10^-4) | Km 2.86 mM (± 0.14) | kcat/Km 4.16 x 10^-4 min^-1 mM^-1 (± 2.02 x 10^-5) | ddG(kJ/mol) –17.08

normalized_value_unit_evidence: kcat: printed Table I cell 1.19 x 10^-3 min^-1; 1 min^-1 is 1/60 s^-1, so 1.19 x 10^-3 / 60 = 0.000019833333333333332 s^-1; the exported value is 0.0005183333 s^(-1). Km: printed Table I cell 2.86 mM; already in mM, no unit conversion applies; the exported value is 2.8600000000000003 mM. kcat/Km: Printed Table I kcat/Km cell 4.16 x 10^-4 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 4.16 x 10^-4 / 60 = 0.000006933333333333334 s^-1 mM^-1. The live export row stores no kcat_over_km field for this identity. Quotient disclosure for this row: 0.000019833333333333332 / 2.86 = 0.000006934731934731935 s^-1 mM^-1, against the printed efficiency cell 0.000006933333333333334 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Type row W429A, Substrate row ONPG-6-P: kcat = 1.19 x 10^-3 min^-1 (printed error ± 4.82 x 10^-4); Km = 2.86 mM (printed error ± 0.14); printed kcat/Km = 4.16 x 10^-4 min^-1 mM^-1 (printed error ± 2.02 x 10^-5); ddG = –17.08 kJ/mol.


row_label: Table I, Type row W429A, Substrate row ONPG-6-P

table_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol)


column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row W429A, Substrate row ONPGlc-6-P; column kcat (min-1) = 3.11 x 10^-2 ± 2.54 x 10^-3; column Km (mM) = 9.83 ± 0.64; column kcat/Km (min-1 mM-1) = 3.16 x 10^-3 ± 4.98 x 10^-4; column ddG (kJ/mol) = –7.53. captured primary segment: W429A | ONPGlc-6-P | kcat 3.11 x 10^-2 min^-1 (± 2.54 x 10^-3) | Km 9.83 mM (± 0.64) | kcat/Km 3.16 x 10^-3 min^-1 mM^-1 (± 4.98 x 10^-4) | ddG(kJ/mol) –7.53

raw_value_unit_evidence: Table I, Type row W429A, Substrate row ONPGlc-6-P: kcat = 3.11 x 10^-2 min^-1 (printed error ± 2.54 x 10^-3); Km = 9.83 mM (printed error ± 0.64); printed kcat/Km = 3.16 x 10^-3 min^-1 mM^-1 (printed error ± 4.98 x 10^-4); ddG = –7.53 kJ/mol.


organism: Thermotoga neapolitana

sequence_source: UniProtKB direct REST check: B9K7M5


substrate_name: Cellobiose


substrate_name: H2O; Cellobiose

substrate: H2O; Cellobiose


substrate_name: p-Nitrophenyl-beta-D-glucoside

substrate: p-Nitrophenyl-beta-D-glucoside


organism: uncultured rumen bacterium

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB direct REST check: G3BJX4

substrate: 4-nitrophenyl beta-D-glucopyranoside


sequence_source: UniProtKB direct REST check: G3BJX3


organism: Bacillus amyloliquefaciens

substrate_name: lactose

sequence_source: UniProtKB REST direct lookup for A0A7S8BFT0

proof_lines:
pH 8, 4°C
pH 8, 10°C
pH 8, 45°C

substrate: lactose


organism: Lactobacillus casei

sequence_source: UniProtKB REST direct lookup for P14696

column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row ONPG-6-P; the Michaelis constant 1.3 comes from the printed column K_m (mM), the turnover number 57 from the printed column k_cat (1/s), and the catalytic efficiency 4.4 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 1.3 mM; already in mM, no unit conversion applies; the exported value is 1.3 mM. kcat: printed cell 57 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 57.0 s^(-1). kcat/Km: printed cell 4.4 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.4 x 10^4 / 1000 = 44.0 s^(-1)*mM^(-1). The exported kcat_over_km 43.84615384615385 s^(-1)*mM^(-1) is the exact quotient of this measurement's own printed cells, 57 / 1.3 = 43.84615384615385, and the printed efficiency cell is that quotient written to the two significant figures the table uses, so the printed cell corroborates the exported value at its own precision.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row ONPG-6-P: Km = 1.3 mM; kcat = 57 1/s; printed kcat/Km = 4.4 x 10^4 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row PNPGlc-6-P; the Michaelis constant 0.6 comes from the printed column K_m (mM), the turnover number 2 from the printed column k_cat (1/s), and the catalytic efficiency 3.0 x 10^3 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.6 mM; already in mM, no unit conversion applies; the exported value is 0.6 mM. kcat: printed cell 2 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 2.0 s^(-1). kcat/Km: printed cell 3.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^3 / 1000 = 3.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 3.3333333333333335 s^(-1)*mM^(-1), the quotient 2 / 0.6 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 3.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row PNPGlc-6-P: Km = 0.6 mM; kcat = 2 1/s; printed kcat/Km = 3.0 x 10^3 M^-1 s^-1.


substrate_name: o-Nitrophenyl beta-D-galactopyranoside 6-phosphate; H2O

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


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row PNPG-6-P; the Michaelis constant 0.2 comes from the printed column K_m (mM), the turnover number 7 from the printed column k_cat (1/s), and the catalytic efficiency 3.4 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.2 mM; already in mM, no unit conversion applies; the exported value is 0.2 mM. kcat: printed cell 7 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 7.0 s^(-1). kcat/Km: printed cell 3.4 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^4 / 1000 = 34.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 35.0 s^(-1)*mM^(-1), the quotient 7 / 0.2 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 34.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row PNPG-6-P: Km = 0.2 mM; kcat = 7 1/s; printed kcat/Km = 3.4 x 10^4 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row ONPGlc-6-P; the Michaelis constant 0.15 comes from the printed column K_m (mM), the turnover number 4 from the printed column k_cat (1/s), and the catalytic efficiency 2.4 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.15 mM; already in mM, no unit conversion applies; the exported value is 0.15 mM. kcat: printed cell 4 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 4.0 s^(-1). kcat/Km: printed cell 2.4 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.4 x 10^4 / 1000 = 24.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 26.666666666666668 s^(-1)*mM^(-1), the quotient 4 / 0.15 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 24.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase L.casei, substrate row ONPGlc-6-P: Km = 0.15 mM; kcat = 4 1/s; printed kcat/Km = 2.4 x 10^4 M^-1 s^-1.


organism: Lactobacillus gasseri


organism: Staphylococcus aureus

sequence_source: UniProtKB REST accession P11175

column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row ONPG-6-P; the Michaelis constant 0.6 comes from the printed column K_m (mM), the turnover number 63 from the printed column k_cat (1/s), and the catalytic efficiency 1.05 x 10^5 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.6 mM; already in mM, no unit conversion applies; the exported value is 0.6 mM. kcat: printed cell 63 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 63.0 s^(-1). kcat/Km: printed cell 1.05 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.05 x 10^5 / 1000 = 105.0 s^(-1)*mM^(-1). The exported kcat_over_km is 105.0 s^(-1)*mM^(-1), which the printed cell reproduces.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row ONPG-6-P: Km = 0.6 mM; kcat = 63 1/s; printed kcat/Km = 1.05 x 10^5 M^-1 s^-1.


organism: Streptococcus mutans

sequence_source: UniProtKB REST accession P50978

substrate: o-Nitrophenyl beta-D-galactopyranoside 6-phosphate; H2O


enzyme_display_name: uridine nucleosidase

organism: Arabidopsis thaliana

substrate_name: uridine

sequence_source: UniProtKB REST accession Q9SJM7

proof_lines: recombinant enzyme expressed in Saccharomyces cerevisiae

proof_lines: recombinant enzyme expressed in Escherichia coli

enzyme: uridine nucleosidase

substrate: uridine


organism: Limosilactobacillus reuteri

substrate_name: Inosine

sequence_source: UniProtKB REST accession A5JJT3

proof_lines: enzyme with His-tag at the C-terminus, pH and temperature not specified in the publication

proof_lines: enzyme with His-tag at the N-terminus, pH and temperature not specified in the publication

substrate: Inosine


organism: Saccharomyces cerevisiae

substrate_name: Unknown

sequence_source: UniProtKB REST accession Q04179

proof_lines: pH 7.5, 37°C, wild-type enzyme, versus uridine

substrate: Unknown


substrate_name: Uridine; H2O

substrate: Uridine; H2O


organism: Zea mays

substrate_name: adenosine

sequence_source: UniProtKB REST accession H9D3U7

assay_conditions_summary: pH 7.5; 303.15 K; buffer 200 mM Tris-HCl

column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Adenosine, enzyme column group ZmNRH2b; column Km (uM) = 111; column kcat (s^-1) = 0.4; column kcat/Km (s^-1 M^-1) = 3.5 x 10^3. captured primary segment: Table II | Adenosine | ZmNRH2b | Km 111 uM | kcat 0.4 s^-1 | kcat/Km 3.5 x 10^3 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 111 uM; 1 uM is 1/1000 mM, so 111 / 1000 = 0.111 mM. kcat: printed Table II cell 0.4 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 0.4 s^(-1). kcat/Km: printed Table II cell 3.5 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.5 x 10^3 / 1000 = 3.5 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Adenosine, enzyme column group ZmNRH2b: Km = 111 uM; kcat = 0.4 s^-1; printed kcat/Km = 3.5 x 10^3 s^-1 M^-1.

substrate: adenosine


column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Inosine, enzyme column group ZmNRH2b; column Km (uM) = 713; column kcat (s^-1) = 4.1; column kcat/Km (s^-1 M^-1) = 5.7 x 10^3. captured primary segment: Table II | Inosine | ZmNRH2b | Km 713 uM | kcat 4.1 s^-1 | kcat/Km 5.7 x 10^3 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 713 uM; 1 uM is 1/1000 mM, so 713 / 1000 = 0.713 mM. kcat: printed Table II cell 4.1 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 4.1 s^(-1). kcat/Km: printed Table II cell 5.7 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.7 x 10^3 / 1000 = 5.7 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Inosine, enzyme column group ZmNRH2b: Km = 713 uM; kcat = 4.1 s^-1; printed kcat/Km = 5.7 x 10^3 s^-1 M^-1.


organism: Lactococcus lactis

substrate_name: o-nitrophenyl-beta-D-galactoside

sequence_variant_note: Resolved canonical sequence from UniProt P11546 direct lookup; variant reconstructed during review and applied mutation signature K435V/Y437F to reconstruct the assayed variant sequence.

proof_lines: K435V/Y437F mutant enzyme, pH 7.5, room temperature

substrate: o-nitrophenyl-beta-D-galactoside


sequence_source: UniProt P11546 direct lookup

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

proof_lines: wild type enzyme, pH 7.5, room temperature


sequence_variant_note: Resolved canonical sequence from UniProt P11546 direct lookup; variant reconstructed during review and applied mutation signature W429A to reconstruct the assayed variant sequence.

proof_lines: W429A mutant enzyme, pH 7.5, room temperature


substrate_name: o-Nitrophenyl-beta-D-galactoside

column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row Wild-type, Substrate row ONPG; column kcat (min-1) = 2.66 x 10^-3 ± 3.13 x 10^-4; column Km (mM) = 0.32 ± 0.20; column kcat/Km (min-1 mM-1) = 8.26 x 10^-3 ± 1.9 x 10^-4; column ddG (kJ/mol) = –. captured primary segment: Wild-type | ONPG | kcat 2.66 x 10^-3 min^-1 (± 3.13 x 10^-4) | Km 0.32 mM (± 0.20) | kcat/Km 8.26 x 10^-3 min^-1 mM^-1 (± 1.9 x 10^-4) | ddG(kJ/mol) –

raw_value_unit_evidence: Table I, Type row Wild-type, Substrate row ONPG: kcat = 2.66 x 10^-3 min^-1 (printed error ± 3.13 x 10^-4); Km = 0.32 mM (printed error ± 0.20); printed kcat/Km = 8.26 x 10^-3 min^-1 mM^-1 (printed error ± 1.9 x 10^-4); ddG = – kJ/mol.

substrate: o-Nitrophenyl-beta-D-galactoside


substrate_name: Xanthosine

sequence_source: UniProtKB:H9D3U7 direct FASTA lookup; organism Zea mays subsp. mays; gene NRH2b; EC 3.2.2.3

substrate: Xanthosine


column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Uridine, enzyme column group ZmNRH2b; column Km (uM) = 514; column kcat (s^-1) = 23.8; column kcat/Km (s^-1 M^-1) = 4.6 x 10^4. captured primary segment: Table II | Uridine | ZmNRH2b | Km 514 uM | kcat 23.8 s^-1 | kcat/Km 4.6 x 10^4 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 514 uM; 1 uM is 1/1000 mM, so 514 / 1000 = 0.514 mM. kcat: printed Table II cell 23.8 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 23.8 s^(-1). kcat/Km: printed Table II cell 4.6 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.6 x 10^4 / 1000 = 46.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Uridine, enzyme column group ZmNRH2b: Km = 514 uM; kcat = 23.8 s^-1; printed kcat/Km = 4.6 x 10^4 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from Reconstructed K289A variant from UniProtKB:H9D3U7 canonical FASTA after direct residue check and applied mutation signature K289A to reconstruct the assayed variant sequence.


proof_lines:
pH 7.5, 30°C, wild-type enzyme W236A
pH 7.5, 30°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from Reconstructed D241Y variant from UniProtKB:H9D3U7 canonical FASTA after direct residue check and applied mutation signature D241Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D241A variant from UniProtKB:H9D3U7 canonical FASTA after direct residue check and applied mutation signature D241A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed W236A variant from UniProtKB:H9D3U7 canonical FASTA after direct residue check and applied mutation signature W236A to reconstruct the assayed variant sequence.


normalized_value_unit_evidence: kcat: printed Table I cell 3.81 x 10^-3 min^-1; 1 min^-1 is 1/60 s^-1, so 3.81 x 10^-3 / 60 = 0.0000635 s^-1; the exported value is 0.00006 s^(-1). Km: printed Table I cell 0.57 mM; already in mM, no unit conversion applies; the exported value is 0.57 mM. kcat/Km: Printed Table I kcat/Km cell 6.66 x 10^-3 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6.66 x 10^-3 / 60 = 0.000111 s^-1 mM^-1. The exported value is 0.00010526315789473685 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.0000635 / 0.57 = 0.00011140350877192984 s^-1 mM^-1, against the printed efficiency cell 0.000111 s^-1 mM^-1.

row_label: Table I, Type row K435V/Y437F, Substrate row ONPG


column_label: Table I: Kinetic parameters of wild-type and mutant 6-phospho-beta-galactosidases for hydrolysis of ONPG, ONPG-6-P, ONPGlc-6-P, PNPG-6-P and PNPGlc-6-P at room temperature in sodium phosphate buffer, pH 7.5 (Protein Engineering 2000, 13(7):515-518); printed column heads Type | Substrate | kcat (min-1) | Km (mM) | kcat/Km (min-1 mM-1) | ddG (kJ/mol). Table I, Type row K435V/Y437F, Substrate row ONPG-6-P; column kcat (min-1) = 7.11 x 10^-3 ± 2.31 x 10^-4; column Km (mM) = 4.89 ± 0.23; column kcat/Km (min-1 mM-1) = 1.45 x 10^-3 ± 1.22 x 10^-4; column ddG (kJ/mol) = –13.96. captured primary segment: K435V/Y437F | ONPG-6-P | kcat 7.11 x 10^-3 min^-1 (± 2.31 x 10^-4) | Km 4.89 mM (± 0.23) | kcat/Km 1.45 x 10^-3 min^-1 mM^-1 (± 1.22 x 10^-4) | ddG(kJ/mol) –13.96

raw_value_unit_evidence: Table I, Type row K435V/Y437F, Substrate row ONPG-6-P: kcat = 7.11 x 10^-3 min^-1 (printed error ± 2.31 x 10^-4); Km = 4.89 mM (printed error ± 0.23); printed kcat/Km = 1.45 x 10^-3 min^-1 mM^-1 (printed error ± 1.22 x 10^-4); ddG = –13.96 kJ/mol.


sequence_source: UniProtKB:P11175 reviewed FASTA

column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row PNPG-6-P; the Michaelis constant 0.3 comes from the printed column K_m (mM), the turnover number 18 from the printed column k_cat (1/s), and the catalytic efficiency 5.9 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.3 mM; already in mM, no unit conversion applies; the exported value is 0.3 mM. kcat: printed cell 18 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 18.0 s^(-1). kcat/Km: printed cell 5.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^4 / 1000 = 59.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 60.0 s^(-1)*mM^(-1), the quotient 18 / 0.3 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 59.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row PNPG-6-P: Km = 0.3 mM; kcat = 18 1/s; printed kcat/Km = 5.9 x 10^4 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row ONPGlc-6-P; the Michaelis constant 0.16 comes from the printed column K_m (mM), the turnover number 9 from the printed column k_cat (1/s), and the catalytic efficiency 5.8 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.16 mM; already in mM, no unit conversion applies; the exported value is 0.16 mM. kcat: printed cell 9 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 9.0 s^(-1). kcat/Km: printed cell 5.8 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.8 x 10^4 / 1000 = 58.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 56.25 s^(-1)*mM^(-1), the quotient 9 / 0.16 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 58.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row ONPGlc-6-P: Km = 0.16 mM; kcat = 9 1/s; printed kcat/Km = 5.8 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11175 canonical FASTA plus selected mutation_signature E160Q and applied mutation signature E160Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phospho-beta-galactosidase(Enzyme) mutant E160Q

substrate: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11175 and applied mutation signature E160Q to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic data of ONPG-6-P utilization (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table III, enzyme row 6-Phospho-beta-galactosidase S.aureus 160 EQ, substrate ONPG-6-P; the Michaelis constant 0.1 comes from the printed column K_m (mM), the turnover number 0.06 from the printed column k_cat (1/s), and the catalytic efficiency 5.6 x 10^2 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.1 mM; already in mM, no unit conversion applies; the exported value is 0.1 mM. kcat: printed cell 0.06 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 0.06 s^(-1). kcat/Km: printed cell 5.6 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.6 x 10^2 / 1000 = 0.56 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 0.6 s^(-1)*mM^(-1), the quotient 0.06 / 0.1 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 0.56 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table III, enzyme row 6-Phospho-beta-galactosidase S.aureus 160 EQ, substrate ONPG-6-P: Km = 0.1 mM; kcat = 0.06 1/s; printed kcat/Km = 5.6 x 10^2 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row PNPGlc-6-P; the Michaelis constant 0.4 comes from the printed column K_m (mM), the turnover number 4 from the printed column k_cat (1/s), and the catalytic efficiency 1.0 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.4 mM; already in mM, no unit conversion applies; the exported value is 0.4 mM. kcat: printed cell 4 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 4.0 s^(-1). kcat/Km: printed cell 1.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.0 x 10^4 / 1000 = 10.0 s^(-1)*mM^(-1). The exported kcat_over_km is 10.0 s^(-1)*mM^(-1), which the printed cell reproduces.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-galactosidase S.aureus, substrate row PNPGlc-6-P: Km = 0.4 mM; kcat = 4 1/s; printed kcat/Km = 1.0 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:H9D3U7 direct REST lookup; H91A reconstructed from the canonical sequence and applied mutation signature H91A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:H9D3U7 direct REST lookup; H249A reconstructed from the canonical sequence and applied mutation signature H249A to reconstruct the assayed variant sequence.


enzyme_display_name: tripeptide aminopeptidase

organism: Homo sapiens

sequence_source: UniProtKB:P09960 direct REST lookup

proof_lines: presence of 0.001 4-(4-[[4-(trifluoromethyl)phenyl]methyl]phenyl)-1,3-thiazol-2-ylamine, pH 7.2, 30°C

proof_lines: presence of 0.001 mM 4-methoxydiphenylmethane, pH 7.2, 30°C

enzyme: tripeptide aminopeptidase


organism: Lactobacillus helveticus

substrate_name: H2O; Met-Gly-Gly

sequence_source: UniProtKB:Q9L4G1 direct REST lookup

substrate: H2O; Met-Gly-Gly


organism: Lactococcus lactis subsp. cremoris

substrate_name: L-Leucyl-L-leucyl-L-leucine

sequence_source: UniProtKB:P0C2T7 direct REST lookup

substrate: L-Leucyl-L-leucyl-L-leucine


substrate_name: L-Leucyl-L-leucyl-L-leucine; H2O

substrate: L-Leucyl-L-leucyl-L-leucine; H2O


organism: Escherichia coli

sequence_source: UniProtKB:P0A725 direct REST lookup


sequence_source: UniProtKB:P0A727 direct exact accession lookup

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


organism: Rhizobium leguminosarum

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1ME43 canonical sequence with direct S214G reconstruction and applied mutation signature S214G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1ME43 canonical sequence with direct W206Q/S214G reconstruction and applied mutation signature W206Q/S214G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1ME43 direct exact accession lookup


enzyme_display_name: agmatinase

substrate_name: Agmatine; H2O

sequence_source: UniProtKB:Q9ZPF5 direct exact accession lookup

enzyme: agmatinase

substrate: Agmatine; H2O


substrate_name: agmatine

sequence_source: UniProtKB:P60651 canonical sequence only; variant sequence not resolved

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

substrate: agmatine


proof_lines: pH 9.5, 37°C, mutant enzyme T154I/Y155N/A156T/N157P-insLTT/G158T/C159S/E160G


sequence_source: UniProtKB:P60651 direct exact accession lookup


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for N139D and applied mutation signature N139D to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme N139D


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for S137C/N139D and applied mutation signature S137C/N139D to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme S137C/N139D


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for D181T and applied mutation signature D181T to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme D181T


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for N130D/S137C and applied mutation signature N130D/S137C to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme N130D/S137C


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for V182E and applied mutation signature V182E to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme V182E


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for S137C and applied mutation signature S137C to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme S137C


sequence_variant_note: Resolved canonical sequence from UniProt P05089 canonical sequence with direct residue-substitution reconstruction for N130D/N139D and applied mutation signature N130D/N139D to reconstruct the assayed variant sequence.

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme N130D/N139D


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from UniProt Q57757 canonical sequence with direct residue-substitution reconstruction for C136A and applied mutation signature C136A to reconstruct the assayed variant sequence.


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


proof_lines: pH 9.5, 37°C, mutant enzyme T188D/E189V/DELTAF190


proof_lines: pH 9.5, 37°C, mutant enzyme T154I/Y155N/A156T/N157P-insLTT


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

smiles: C(CCN=C(N)N)CN


proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme N130D/S137C/N139D

proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme N130D/S137CN139D


proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme I129T/N130Y/T131A/P132del/L133del/T134del


proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme D181T/V182E


proof_lines: pH 9.5, temperature not specified in the publication, mutant enzyme N130D


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q57757 FASTA with row-specific C229A reconstruction and applied mutation signature C229A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q57757 FASTA


smiles: N=C(N)NCCCCN


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q57757 FASTA with row-specific C151S reconstruction and applied mutation signature C151S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q57757 FASTA with row-specific C151S reconstruction


sequence_source: UniProtKB reviewed Q57757 FASTA with row-specific C229A reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q57757 FASTA with row-specific C136A reconstruction and applied mutation signature C136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q57757 FASTA with row-specific C71S reconstruction and applied mutation signature C71S to reconstruct the assayed variant sequence.


enzyme_display_name: signal-recognition-particle GTPase

organism: Mycobacterium tuberculosis

substrate_name: GTP; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA direct accession lookup for P9WGD9 on 2026-06-10 and applied mutation signature D367A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant D367A N-terminal GST-tag

proof_lines: mutant enzyme D367A, in the presence of 10 mM Mg2+, at pH 8.0 and 37°C

enzyme: signal-recognition-particle GTPase

substrate: GTP; H2O


organism: Semliki forest virus

substrate_name: GTP

sequence_source: UniProtKB REST/FASTA direct accession lookup for P08411 on 2026-06-10

substrate: GTP


enzyme_display_name: indolepyruvate decarboxylase

organism: Enterobacter cloacae

sequence_source: UniProtKB P23234 canonical sequence; reviewed Swiss-Prot entry DCIP_ENTCL checked by direct UniProt REST lookup.

enzyme: indolepyruvate decarboxylase


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: 4-Methylbenzoylformic acid

substrate: 4-Methylbenzoylformic acid


substrate_name: 4-Ethylbenzoylformic acid

substrate: 4-Ethylbenzoylformic acid


substrate_name: 4-Methoxybenzoylformic acid

substrate: 4-Methoxybenzoylformic acid


organism: Methylorubrum extorquens

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

proof_lines: at pH 6.5, temperature not specified in the publication


substrate_name: pyruvate

sequence_source: UniProtKB:P23234 direct FASTA lookup; reviewed canonical wild-type sequence.

smiles: CC(=O)C(=O)O

substrate: pyruvate


substrate_name: 4-Chloro-2-Oxobenzeneacetic acid

substrate: 4-Chloro-2-Oxobenzeneacetic acid


substrate_name: alpha-Oxo-benzeneacetic acid

substrate: alpha-Oxo-benzeneacetic acid


sequence_variant_note: Resolved canonical sequence from UniProt Q57757 direct lookup; C71S reconstructed after confirming canonical residue 71 is C. and applied mutation signature C71S to reconstruct the assayed variant sequence.


enzyme_display_name: riboflavin synthase

organism: Unknown

enzyme: riboflavin synthase


substrate_name: L-Glutamate; 2-Oxoadipate; 2-Oxoadipate

proof_lines:
pH 8.0, 37°C isoenzyme AadAT-II
pH 8.0, 37°C
pH 8.0, 37°C, isoenzyme AadAT-II

substrate: L-Glutamate; 2-Oxoadipate; 2-Oxoadipate


enzyme_display_name: adenylyl-sulfate kinase

substrate_name: 3'-phosphoadenosine 5'-phosphosulfate

enzyme: adenylyl-sulfate kinase

substrate: 3'-phosphoadenosine 5'-phosphosulfate


organism: Marinobacter nauticus

substrate_name: hexadecanol

protein_accession_database: NCBI Protein

sequence_source: GenBank EF219377.1 CDS translation; protein ABO21021.1; PMID 17351040 Table 1 WS2

smiles: CCCCCCCCCCCCCCCCO

substrate: hexadecanol


enzyme_display_name: beta-amylase

organism: Glycine max

substrate_name: starch

proof_lines:
pH 5.4-6.0, major isozyme
soluble

substrate: starch


enzyme_display_name: cytokinin dehydrogenase

organism: Arabidopsis thaliana

substrate_name: isopentenyladenine

source_db: uniprot

enzyme: cytokinin dehydrogenase

substrate: isopentenyladenine

source: uniprot


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

substrate_name: palmitoyl-CoA (C(16), in wax synthase)

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

assay_conditions_summary: cofactor CoA

substrate: palmitoyl-CoA (C(16), in wax synthase)


organism: Mus musculus


organism: Bacillus subtilis (strain 168)


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: 6,7-dimethyl-8-(1-D-ribityl)lumazine (at pH 7.2 and 37 degrees Celsius)


enzyme_display_name: 2-aminoadipate transaminase

organism: Homo sapiens

substrate_name: aminoadipate

substrate: aminoadipate


substrate_name: CTP

substrate: CTP


enzyme_display_name: cephalosporin-C deacetylase

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

substrate_name: p-nitrophenyl-acetate

enzyme: cephalosporin-C deacetylase

substrate: p-nitrophenyl-acetate


enzyme_display_name: phospholipase D

substrate_name: Unknown

enzyme: phospholipase D

substrate: Unknown


substrate_name: pNppp (isoform 1)

substrate: pNppp (isoform 1)


organism: Streptomyces chromofuscus


organism: Lactococcus lactis subsp. cremoris

substrate_name: tripeptide Leu-Leu-Leu

substrate: tripeptide Leu-Leu-Leu


substrate_name: leukotriene A4

substrate: leukotriene A4


organism: Xenopus laevis

substrate_name: LTA4 at room temperature, pH 7.8

substrate: LTA4 at room temperature, pH 7.8


substrate_name: agmatine

substrate: agmatine


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: pyruvate

substrate: pyruvate


organism: Rattus norvegicus

substrate_name: L-kynurenine

substrate: L-kynurenine


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: 2-oxoisovalerate (at 45 degrees Celsius and pH 7.5)


substrate_name: adenosine 5'-phosphosulfate

assay_conditions_summary: cofactor ATP

substrate: adenosine 5'-phosphosulfate


substrate_name: adenylyl sulfate

substrate: adenylyl sulfate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


organism: Crithidia fasciculata

substrate_name: inosine

proof_lines: kcat is 32 sec(-1) with inosine as substrate. kcat is 243 sec(-1) with 5-methyluridine as substrate.

substrate: inosine


organism: Leishmania major

proof_lines: kcat is 119 sec(-1) with inosine as substrate. kcat is 32 sec(-1) with uridine as substrate. kcat is 0.6 sec(-1) with guanosine as substrate. kcat is 0.6 sec(-1) with adenosine as substrate. kcat is 0.4 sec(-1) with cytidine as substrate.


proof_lines: kcat is 355 sec(-1) with GGF tripeptide as substrate. kcat is 437 sec(-1) with GGA tripeptide as substrate. kcat is 850 sec(-1) with GAA tripeptide as substrate. kcat is 1050 sec(-1) with GAY tripeptide as substrate. kcat is 240 sec(-1) wit


organism: Lactococcus lactis subsp. hordniae

proof_lines: kcat is 639 sec(-1) with GGF tripeptide as substrate. kcat is 915 sec(-1) with GGA tripeptide as substrate. kcat is 1015 sec(-1) with GAA tripeptide as substrate. kcat is 1219 sec(-1) with GAY tripeptide as substrate. kcat is 373 sec(-1) wi


organism: Lactococcus lactis subsp. lactis

substrate_name: AAA tripeptide

proof_lines: kcat is 163 sec(-1) with AAA tripeptide as substrate. kcat is 616 sec(-1) with GAA tripeptide as substrate. kcat is 713 sec(-1) with AGA tripeptide as substrate. kcat is 730 sec(-1) with AAG tripeptide as substrate. kcat is 507 sec(-1) with

substrate: AAA tripeptide


organism: Escherichia coli (strain K12)

substrate_name: UDP-3-O-myristoyl-N-acetylglucosamine (at 30 degrees Celsius)

proof_lines: kcat is 3.3 sec(-1) at 30 degrees Celsius. kcat is 0.09 sec(-1) at 1 degree Celsius.


enzyme_display_name: pullulanase

organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

substrate_name: para-nitrophenyl-alpha-D-maltopentaoside (pNP-M5) (at 25 degrees Celsius)


enzyme_display_name: glucan 1,4-beta-glucosidase

organism: Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (pNPGal) (at pH 5.5 and 75 degrees Celsius)

proof_lines: kcat is 4522 sec(-1) with pNPGal as substrate. kcat is 3750.6 sec(-1) with pNPGlu as substrate. kcat is 944.3 sec(-1) with pNPC as substrate. kcat is 652.6 sec(-1) with pNPX as substrate. kcat is 2149 sec(-1) with cellobiose as substrate.


organism: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E)

substrate_name: cellobiose

proof_lines: kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of cellobiose, cellotriose and cellotetraose, respectively.

substrate: cellobiose


organism: Arabidopsis thaliana

substrate_name: uridine

proof_lines: kcat is 2.65 sec(-1) with xanthosine as substrate (PubMed:30787180). kcat is 33.5 sec(-1) with uridine as substrate (PubMed:30787180). kcat is 23.3 sec(-1) with xanthosine as substrate (when in complex with URH2) (PubMed:30787180). kcat is

substrate: uridine


substrate_name: xanthosine (when in complex with URH2)

proof_lines: kcat is 23.3 sec(-1) with xanthosine as substrate (when in complex with URH2) (PubMed:30787180). kcat is 55.3 sec(-1) with uridine as substrate (when in complex with URH2) (PubMed:30787180). kcat is 42.3 sec(-1) with inosine as substrate (w

substrate: xanthosine (when in complex with URH2)


organism: Caenorhabditis elegans

substrate_name: inosine (at pH 7.0 and 37 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 0.79 sec(-1) with inosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783). kcat is 0.203 sec(-1) with inosine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:28218438). kcat is 0.78 sec(-1) with adenosine a


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


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: N(1)-aminopropylagmatine (at pH 7.5 and 70 degrees Celsius)

proof_lines: kcat is 1.86 sec(-1) for ureohydrolase activity with agmatine as substrate (at pH 7.5 and 70 degrees Celsius). kcat is 1.01 sec(-1) for ureohydrolase activity with N(1)-aminopropylagmatine as substrate (at pH 7.5 and 70 degrees Celsius).


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: GTP

proof_lines: kcat is 0.012 sec(-1) for GTP hydrolysis (PubMed:33412199). kcat is 0.007 sec(-1) for ATP hydrolysis (PubMed:33412199).

substrate: GTP


organism: Bacillus subtilis

proof_lines:
light enzyme, Bacillus subtilis H94
heavy enzyme, Bacillus subtilis H94
pH 7.0, 37°C


organism: Brucella abortus


organism: Eremothecium ashbyi

substrate_name: Unknown

substrate: Unknown


organism: Eremothecium gossypii


organism: Escherichia coli

proof_lines:
per subunit
pH 7.5, 37°C
pH 7.0, 27°C


proof_lines: pH 6.9, 25°C, recombinant mutant H102Q, steady-state conditions


proof_lines: with 2,3-dimethoxy-5-methyl-p-benzoquinone, pH 7.0, 37°C


organism: Nicotiana tabacum

proof_lines: transgenic plant cells conditionally overexpressing isopentenyltransferase, cell culture medium induced by tetracycline, pH 6.0, 37°C

proof_lines: transgenic plant cells conditionally overexpressing isopentenyltransferase, cell extract induced by tetracycline, pH 6.0, 37°C

proof_lines: transgenic plant cells conditionally overexpressing isopentenyltransferase, cell culture medium, pH 6.0, 37°C


organism: Zea mays

proof_lines: pH 5.0, temperature not specified in the publication

proof_lines: Km above 0.25 mM, pH 7.0, temperature not specified in the publication


organism: Bos taurus

substrate_name: 1-Hexadecanol; Palmitoyl-CoA

substrate: 1-Hexadecanol; Palmitoyl-CoA


organism: Streptomyces coelicolor

substrate_name: acetyl-CoA

proof_lines: pH and temperature not specified in the publication

substrate: acetyl-CoA


organism: Saccharomyces cerevisiae

substrate_name: L-phenylalanine

proof_lines: pH 7.0, temperature not specified in the publication

substrate: L-phenylalanine


organism: Thermus thermophilus


substrate_name: adenosine 5'-phosphosulfate

proof_lines: reduced wild type enzyme, at pH 7.5 and 17°C

proof_lines: oxidized wild type enzyme, at pH 7.5 and 17°C


mutation_type: deletion

proof_lines: N-terminal truncation variant APSKDELTA96, at pH 7.5 and 17°C


organism: Chlamydomonas reinhardtii

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


organism: Bacillus subtilis (strain 168)


organism: Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b)

substrate_name: oNPbetagal6P (at pH 7.5)

substrate: oNPbetagal6P (at pH 7.5)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Fusobacterium nucleatum subsp. polymorphum

substrate_name: dipeptide Leu-Ala

sequence: MDXKXYVDLKERFLRYVKFN

substrate: dipeptide Leu-Ala


organism: Homo sapiens

substrate_name: Pro-Gly-Pro

substrate: Pro-Gly-Pro


organism: Lactobacillus helveticus

substrate_name: tripeptide Met-Gly-Gly

substrate: tripeptide Met-Gly-Gly


substrate_name: adenosine 5-phosphosulfate

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: adenosine 5-phosphosulfate


organism: Geobacillus stearothermophilus

substrate: adenosine 5'-phosphosulfate


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8.0, 37°C, PAPSS 2a
pH 8.0, 37°C, PAPSS 1
pH 8.0, 37°C, PAPSS 2b

substrate: ATP


substrate_name: adenylyl sulfate

substrate: adenylyl sulfate


proof_lines: value is below 0.002 for a deletion mutant lacking the first 34 amino acids of the N-terminus, delta34N


proof_lines: deletion mutant lacking the first 50 amino acids of the N-terminus, delta50N


proof_lines: value is below 0.002 for wildtype adenylyl sulfate


organism: Oryza sativa

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


proof_lines: mutant enzyme C36A/C69A, at pH 8.0 and 25°C


organism: Penicillium chrysogenum

proof_lines:
pH 8.0, 30°C
pH 8.1, 30°C
ATP in form of MgATP2-


organism: Pyropia yezoensis


organism: Escherichia coli

proof_lines: pH 6.9, 25°C, recombinant wild-type enzyme, steady-state conditions


organism: Mycobacterium tuberculosis

proof_lines: noncompetitive mechanism, compound has a kis value of 0.0087 mM and moderate antibiotic activity against both Mycobacterium tuberculosis replicating phenotype and non-replicating persistent phenotype

proof_lines: in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27°C


organism: Spinacia oleracea


organism: Rattus norvegicus


organism: Amycolatopsis lactamdurans

substrate_name: cephalosporin C

substrate: cephalosporin C


organism: Bacillus pumilus


organism: Bacillus subtilis

substrate_name: cephalothin

proof_lines:
strain SHS 0133, FERM BP-2755
recombinant enzyme, 30°C
strain ATCC6633

substrate: cephalothin


organism: Citrus sp.


organism: Hapsidospora chrysogena


organism: Rhodotorula glutinis

substrate_name: 7-aminocephalosporanic acid

substrate: 7-aminocephalosporanic acid


organism: Rhodotorula toruloides


organism: Actinomadura sp.

substrate_name: phosphatidylcholine

substrate: phosphatidylcholine


organism: Arachis hypogaea

proof_lines: transphosphaditylation in presence of methanol

proof_lines: in presence of 10 mM CaCl2, 4 mM deoxycholate


organism: Bos taurus

substrate_name: H2O; Phosphatidylcholine

proof_lines: transphosphaditylation in presence of 400 mM ethanol

substrate: H2O; Phosphatidylcholine


organism: Brassica napus


organism: Brassica oleracea

substrate_name: dihexanoylphosphatidylcholine

substrate: dihexanoylphosphatidylcholine


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by PKCalpha + RhoA N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by PKCalpha + RhoA


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by RhoA N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by RhoA


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Arf1 + RhoA N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Arf1 + RhoA


proof_lines: full length enzyme stimulated by PKCalpha


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by PKCalpha + Cdc42 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by PKCalpha + Cdc42


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Arf1 + PKCalpha N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Arf1 + PKCalpha


organism: Homo sapiens


organism: Oryza sativa

sequence_source: UniProtKB reviewed Q43007 (PLDA1_ORYSJ), linked to PMID 7551587


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Cdc42 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Cdc42


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Arf-1 + Cdc42 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Arf-1 + Cdc42


mutation_signature: N-terminally truncated enzyme PLD1 / unstimulated N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, unstimulated


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by PKCalpha + Rac1 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by PKCalpha + Rac1


organism: Thermobifida fusca


organism: Arabidopsis thaliana

sequence_source: UniProtKB:P69834 reviewed Swiss-Prot; PMID 10841550 cloned the Arabidopsis thaliana ispD-like cDNA and reports a 302-aa protein matching P69834.


organism: Escherichia coli

substrate_name: 2-C-methyl-D-erythritol-4-phosphate; CTP; 2-C-methyl-D-erythritol 4-phosphate


organism: Francisella tularensis

sequence_source: UniProtKB:A0AAI8BIR0 unreviewed TrEMBL; PMID 21694781 full text identifies F. tularensis subsp. holarctica LVS ispD / FTL_1525 as the cloned enzyme.


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WKG9 reviewed Swiss-Prot; PMID 18047786 identifies recombinant IspD from Mycobacterium tuberculosis H37Rv.

proof_lines: slightly lower than from bacterial and plant sources


organism: Streptomyces coelicolor

sequence_source: UniProtKB:Q9L0Q8 reviewed Swiss-Prot; PMID 11408165 cloned and characterized Streptomyces coelicolor MEP pathway genes including the EC 2.7.7.60 cytidylyltransferase.


organism: Brassica oleracea var. capitata

substrate_name: lysophosphatidylcholine

proof_lines:
at 4 mM Ca2+
at 40 mM Ca2+
transphosphatidylation

substrate: lysophosphatidylcholine


organism: Daucus carota

substrate_name: p-Nitrophenylphosphorylcholine

substrate: p-Nitrophenylphosphorylcholine


organism: Glycine max


substrate_name: N-palmitoyl-phosphatidylethanolamine

proof_lines: mutant D389N, 37°C, pH 7.4, presence of 10 mM MgCl2

substrate: N-palmitoyl-phosphatidylethanolamine


proof_lines: mutant S152A, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: wild-type, 37°C, pH 7.4, presence of 10 mM MgCl2


organism: Rattus norvegicus

proof_lines: mutant C222S, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant C237S, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant C224S, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant C288S, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant DELTAN55, 37°C, pH 7.4, presence of 10 mM MgCl2


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Arf-1 + Rac1 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Arf-1 + Rac1


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by PKCalpha N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by PKCalpha


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Arf-1 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Arf-1


mutation_signature: N-terminally truncated enzyme PLD1 / stimulated by Rac1 N-terminally truncated enzyme PLD1

proof_lines: N-terminally truncated enzyme PLD1, stimulated by Rac1


proof_lines: mutant H331N, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant C170S, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant 387stop, 37°C, pH 7.4, presence of 10 mM MgCl2


proof_lines: mutant C255S, 37°C, pH 7.4, presence of 10 mM MgCl2


organism: Streptomyces antibioticus

assay_conditions_summary: pH 5.6; 310.15 K; buffer sodium acetate

proof_lines: mutant enzyme 187F/191R/385Y, in sodium acetate buffer (50 mM, pH 5.6), at 37°C

proof_lines: mutant enzyme 187H/191Y/385R, in sodium acetate buffer (50 mM, pH 5.6), at 37°C

proof_lines: mutant enzyme 187T/191Y/385R, in sodium acetate buffer (50 mM, pH 5.6), at 37°C


proof_lines: wild type enzyme, in sodium acetate buffer (50 mM, pH 5.6), at 37°C


organism: Streptomyces chromofuscus

substrate_name: bis(p-nitrophenyl)phosphate; dibutyroylphosphatidylcholine; phosphatidylcholine; diheptanoylphosphatidylcholine; sphingomyelin; lysophosphatidylcholine

assay_conditions_summary: pH 8

proof_lines:
pH 8.0, 0.065 mM Ca2+
reaction with PLD37/18


organism: Streptomyces hachijoensis

substrate_name: phosphatidylethanolamine

substrate: phosphatidylethanolamine


organism: Streptomyces hiroshimensis

substrate_name: egg phosphatidylcholine

proof_lines: pH 6.0, 60°C, enzyme from wild-type strain SK43.001

substrate: egg phosphatidylcholine


proof_lines: pH 6.0, 60°C, high-yielding mutant enzyme, strain SK43.001-11


organism: Streptomyces olivochromogenes


organism: Streptomyces septatus

substrate_name: phosphatidyl-p-nitrophenol

sequence_source: NCBI Protein BAB69062.1; DBSOURCE AB058783.1

proof_lines:
pH 5.5, hydrolysis
pH 5.5, transphosphatidylation

substrate: phosphatidyl-p-nitrophenol


organism: Streptomyces sp.


organism: Streptomyces tendae


organism: Sus scrofa


organism: Bacillus cereus

substrate_name: maltoheptaose

enzyme: beta-amylase

substrate: maltoheptaose


organism: Curculigo pilosa

substrate_name: amylose

proof_lines:
from potato
soluble starch

substrate: amylose


organism: Hordeum vulgare

substrate_name: starch

proof_lines: pH 5, 40°C, soluble starch, D165E mutant of Sd2L

substrate: starch


proof_lines: pH 5, 40°C, soluble starch, L347S and R115C mutants of Sd2L


proof_lines: pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L

proof_lines: pH 5, 40°C, soluble starch, wild-type Sd1

proof_lines: pH 5, 40°C, soluble starch, wild-type Sd2L


proof_lines: pH 5, 40°C, soluble starch, V430A mutant of Sd2L


proof_lines: pH 5, 40°C, soluble starch, D165E and V430A mutants of Sd2L


proof_lines: pH 5, 40°C, soluble starch, R115C mutant of Sd2L


proof_lines: pH 5, 40°C, soluble starch, V233A mutant of Sd1

proof_lines: pH 5, 40°C, soluble starch, V233A mutant of Sd2L


proof_lines: pH 5, 40°C, soluble starch, L347S mutant of Sd2L


substrate_name: pullulan

substrate: pullulan


organism: Thermoanaerobium sp.


organism: Thermococcus litoralis

substrate_name: 4-nitrophenyl alpha-D-maltotrioside

proof_lines:
pH 5.6, 98°C, no metal added
pH 5.6, 98°C, 5 mM Ca2+

substrate: 4-nitrophenyl alpha-D-maltotrioside


organism: unidentified


organism: Aspergillus niger

substrate_name: cellobiose

proof_lines:
at 50ºC, pH 4.9
at 40ºC, pH 4.9
at 60ºC, pH 4.9

substrate: cellobiose


organism: Cellulomonas fimi

substrate_name: Unknown

substrate: Unknown


substrate_name: maltohexaose

substrate: maltohexaose


organism: Ipomoea batatas

substrate_name: maltal

substrate: maltal


organism: Solanum tuberosum

substrate_name: p-nitrophenylmaltopentaoside

substrate: p-nitrophenylmaltopentaoside


organism: Vicia faba

substrate_name: maltodextrin

proof_lines:
with 50 glucose equivalents per chain
with 98 glucose equivalents per chain
with 9 glucose equivalents per chain

substrate: maltodextrin


organism: Bacillus acidopullulyticus


organism: Bacillus deramificans

proof_lines:
pH 4.5, 60°C, 60 mM Mg2+
pH 4.5, 60°C, without Mg2+


organism: Bacillus sp. (in: firmicutes)


proof_lines: pH 6.8, 45°C, recombinant wild-type enzyme


organism: Bacillus subtilis


organism: Geobacillus stearothermophilus

proof_lines: recombinant wild-type enzyme, pH 6.5, 60°C


proof_lines: recombinant mutant G250P/T252S/G253T/N255K, pH 6.5, 60°C


organism: Klebsiella aerogenes

sequence_source: UniProtKB P07811 reviewed pullulanase; sequence not promoted because the row remains manual


organism: Metabacillus indicus

km_unit: mg/mL

sequence_source: NCBI Protein KEZ51383.1; GenBank OP585545.1; PMID 37119334 / PMCID PMC10148936


organism: Oryza sativa

substrate_name: amylopectin

substrate: amylopectin


organism: Pyrococcus furiosus

proof_lines:
pH 5.6, 98°C, 5 mM Ca2+
pH 5.6, 98°C, no metal added


organism: Nakazawaea wickerhamii

substrate_name: p-nitrophenyl-beta-D-glucopyranoside

substrate: p-nitrophenyl-beta-D-glucopyranoside


organism: Paenibacillus curdlanolyticus

substrate_name: Barley beta-glucan

assay_conditions_summary: pH 6

proof_lines: at pH 6.0, temperature not specified in the publication

substrate: Barley beta-glucan


organism: Pseudomonas fluorescens

substrate_name: cellohexaose

substrate: cellohexaose


organism: Ruminococcus albus

substrate_name: p-nitrophenyl-beta-D-glucoside

substrate: p-nitrophenyl-beta-D-glucoside


organism: Stereum hirsutum

assay_conditions_summary: pH 4.5; 338.15 K; buffer 100 mM sodium acetate

proof_lines: in 100 mM sodium acetate buffer (pH 4.5), at 65°C


organism: Talaromyces funiculosus

substrate_name: cellopentaose

substrate: cellopentaose


organism: Cellulomonas fimi


organism: Chaetomium globosum

substrate_name: alpha-cellulose

assay_conditions_summary: pH 5

substrate: alpha-cellulose


organism: Hordeum vulgare


organism: Komagataeibacter xylinus

substrate_name: cellotriose

substrate: cellotriose


organism: Lactobacillus gasseri


organism: Lactococcus cremoris


organism: Lactococcus lactis


organism: Lactococcus lactis subsp. cremoris

substrate_name: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


organism: Lactococcus lactis subsp. lactis

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


proof_lines: SABIO-RK modifier species: 6-phospho-beta-galactosidase(Enzyme) mutant Lac- Gal d

substrate: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


organism: Trichoderma reesei


organism: uncultured bacterium

substrate_name: 4-nitrophenyl beta-D-cellobioside

assay_conditions_summary: pH 5.5; 338.15 K; buffer pH 5.5 citrate

substrate: 4-nitrophenyl beta-D-cellobioside


organism: Vibrio cholerae serotype O1

substrate_name: p-nitrophenyl glucoside

substrate: p-nitrophenyl glucoside


organism: Xylanibacter ruminicola

substrate_name: arbutin

substrate: arbutin


organism: Klebsiella sp.

proof_lines:
with strain CT-1
with strain RE1755A


organism: Lacticaseibacillus casei


organism: Leptotrichia buccalis


organism: Staphylococcus aureus


organism: Streptococcus mutans


organism: Arabidopsis thaliana

substrate_name: Inosine

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

substrate: Inosine


organism: Escherichia coli

substrate_name: adenosine

proof_lines: pH 7.2, 32°C, recombinant His-tagged enzyme

substrate: adenosine


organism: Hordeum vulgare

substrate_name: uridine

substrate: uridine


organism: Saccharomyces cerevisiae

substrate_name: nicotinic acid riboside methyl ester

sequence_source: UniProtKB reviewed accession Q04179 (URH1_YEAST), retrieved by direct EC 3.2.2.3 + Saccharomyces cerevisiae lookup.

assay_conditions_summary: pH 7; cofactor NAD+

substrate: nicotinic acid riboside methyl ester


organism: Vigna radiata var. radiata


organism: Zea mays

substrate_name: Xanthosine

substrate: Xanthosine


substrate_name: Unknown

substrate: Unknown


organism: Bacillus subtilis

substrate_name: Met-Ala-Ser

proof_lines: pH 7.4, 55°C, in presence of 0.004 mM Zn2+

proof_lines: pH 7.4, 55°C, in presence of 0.004 mM Co2+

substrate: Met-Ala-Ser


organism: Homo sapiens


proof_lines:
pH 5.0, 37°C, wild-type enzyme
calculated value, wild type enzyme


organism: Lactococcus lactis

substrate_name: Gly-Gly-Phe

substrate: Gly-Gly-Phe


organism: Lactococcus lactis subsp. lactis

substrate_name: H2O; Glycyl-glycyl-L-phenylalanine

sequence_source: UniProtKB Q76HM5 direct lookup; linked by lit_pubmed:16233215 and ATCC 13675/diacetylactis search

substrate: H2O; Glycyl-glycyl-L-phenylalanine


organism: Latilactobacillus sakei

substrate_name: Phe-Gly-Gly

substrate: Phe-Gly-Gly


organism: Macaca fuscata

substrate_name: Leu-Gly-Gly

substrate: Leu-Gly-Gly


organism: Oryctolagus cuniculus


sequence_variant_note: Resolved canonical sequence from NCBI PubMed elink PMID 17176046 -> Protein 16128089; RefSeq NP_414638.1; UniProtKB/Swiss-Prot P0A725 and applied mutation signature D197E to reconstruct the assayed variant sequence.

proof_lines:
D197E mutant
D197E mutant, 5fold decrease


sequence_variant_note: Resolved canonical sequence from NCBI PubMed elink PMID 17176046 -> Protein 16128089; RefSeq NP_414638.1; UniProtKB/Swiss-Prot P0A725 and applied mutation signature F192A to reconstruct the assayed variant sequence.

proof_lines:
F192A mutant
F192A mutant, 1200fold decrease


sequence_variant_note: Resolved canonical sequence from NCBI PubMed elink PMID 17176046 -> Protein 16128089; RefSeq NP_414638.1; UniProtKB/Swiss-Prot P0A725 and applied mutation signature K143A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI PubMed elink PMID 17176046 -> Protein 16128089; RefSeq NP_414638.1; UniProtKB/Swiss-Prot P0A725 and applied mutation signature T191A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI PubMed elink PMID 17176046 -> Protein 16128089; RefSeq NP_414638.1; UniProtKB/Swiss-Prot P0A725 and applied mutation signature K239A to reconstruct the assayed variant sequence.

proof_lines:
K239A mutant
K239A mutant, 575fold decrease


sequence_variant_note: Resolved canonical sequence from NCBI PubMed elink PMID 17176046 -> Protein 16128089; RefSeq NP_414638.1; UniProtKB/Swiss-Prot P0A725 and applied mutation signature D197A to reconstruct the assayed variant sequence.

proof_lines:
D197A mutant
D197A mutant, 5fold decrease


organism: Aquifex aeolicus


proof_lines: pH 7.5, 30°C, mutant enzyme D246A, steady-state


proof_lines: pH 7.5, 30°C, mutant enzyme E78A/H265A, steady-state


proof_lines: pH 7.5, 30°C, mutant enzyme H265A, steady-state


proof_lines: pH 7.5, 30°C, mutant enzyme E78A, steady-state


proof_lines:
H19A mutant
H19A mutant, 575fold decrease


proof_lines: pH 7.5, 30°C, wild-type Zn2+-containing enzyme, steady-state


proof_lines:
H19Q mutant
H19Q mutant, 135fold decrease


proof_lines:
H19Y mutant
H19Y mutant, 350fold decrease


proof_lines:
mutant C63A Zn2+-LpxC, pH 7.5, 30°C
mutant C63A Fe2+-LpxC, pH 7.5, 30°C


organism: Porphyromonas gingivalis

proof_lines: mutant enzyme E363A, in 20 mM Tris-HCl (pH 7.0) at 37°C


substrate_name: Gly-Ala-Pro-beta-naphthylamide

proof_lines: wild type enzyme, in 20 mM Tris-HCl (pH 7.0) at 37°C

substrate: Gly-Ala-Pro-beta-naphthylamide


substrate_name: Ala-Phe-Pro-beta-naphthylamide

proof_lines: mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0) at 37°C

substrate: Ala-Phe-Pro-beta-naphthylamide


organism: Rattus norvegicus


organism: Serratia marcescens

assay_conditions_summary: pH 7; 310.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer (pH 7.0), at 37°C


organism: Sus scrofa

substrate_name: Gly-Gly-Gly

substrate: Gly-Gly-Gly


organism: Neurospora crassa

substrate_name: agmatine

substrate: agmatine


organism: Pyrococcus horikoshii

sequence_source: UniProtKB reviewed accession O57839 direct EC+organism lookup


organism: Clostridium butyricum


organism: Escherichia coli


organism: Evernia prunastri


organism: Klebsiella pneumoniae

proof_lines: recombinant mutant A387L, pH and temperature not specified in the publication


proof_lines: recombinant mutant Q383M, pH and temperature not specified in the publication


organism: Saccharomyces cerevisiae

substrate_name: Indolepyruvate

substrate: Indolepyruvate


organism: Sulfolobus sp.


organism: Enterobacter cloacae

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB reviewed accession P23234 after direct EC+organism lookup and PMID 15835904 Q383T row note and applied mutation signature Q383T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P23234 from direct EC+organism lookup


substrate_name: pyruvate

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB reviewed accession P23234 after direct EC+organism lookup and PMID 15835904 H115K row note and applied mutation signature H115K to reconstruct the assayed variant sequence.

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB reviewed accession P23234 after direct EC+organism lookup and PMID 15835904 E52D row note and applied mutation signature E52D to reconstruct the assayed variant sequence.


substrate_name: benzoylformic acid

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB reviewed accession P23234 after direct EC+organism lookup and PMID 15835904 D29E row note and applied mutation signature D29E to reconstruct the assayed variant sequence.

substrate: benzoylformic acid


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


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

proof_lines: recombinant mutant A387I, pH and temperature not specified in the publication


proof_lines: recombinant mutant A387I/F388W, pH and temperature not specified in the publication


proof_lines: recombinant mutant T290L, pH and temperature not specified in the publication


proof_lines: recombinant mutant F388W, pH and temperature not specified in the publication


proof_lines: recombinant mutant V542I, pH and temperature not specified in the publication


proof_lines: recombinant mutant L546W, pH and temperature not specified in the publication