substrate_name: H+; 3-Dehydro-L-gulonate 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 direct accession check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature K64A/E112Q/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64A/E112Q/H136A

substrate: H+; 3-Dehydro-L-gulonate 6-phosphate


organism: Escherichia coli

substrate_name: 3-Dehydro-L-gulonate 6-phosphate

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64A/E112Q/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64A/E112Q/H136A'; column 'kcat (s-1)' = 2.9; column 'KM (M)' = 5.5 x 10^-4; column 'kcat/KM (M-1 s-1)' = 5.3 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.9 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 2.9 s^(-1). Km: printed Table 1 cell 5.5 x 10^-4 M; 1 M is 1000 mM, so 5.5 x 10^-4 x 1000 = 0.55 mM. kcat/Km: printed Table 1 cell 5.3 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.3 x 10^3 / 1000 = 5.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'K64A/E112Q/H136A': kcat = 2.9 s-1; KM = 5.5 x 10^-4 M; printed kcat/KM = 5.3 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'K64A/E112Q/H136A' (the mutant K64A/E112Q/H136A entry of the single kinetic table in this article)

data_origin: experimental

substrate: 3-Dehydro-L-gulonate 6-phosphate

status: corrected

source: oed


substrate_name: 3-Dehydro-L-gulonate 6-phosphate; H+

kcat_over_km_display: Not reported

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

sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 direct accession check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature E112Q to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant E112Q

substrate: 3-Dehydro-L-gulonate 6-phosphate; H+


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 direct accession check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature E112Q/H136A/R139V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant E112Q/H136A/R139V


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature D67N to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'D67N'; column 'kcat (s-1)' = 1.1; column 'KM (M)' = 4.1 x 10^-4; column 'kcat/KM (M-1 s-1)' = 2.7 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.1 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 1.1 s^(-1). Km: printed Table 1 cell 4.1 x 10^-4 M; 1 M is 1000 mM, so 4.1 x 10^-4 x 1000 = 0.41 mM. kcat/Km: printed Table 1 cell 2.7 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^3 / 1000 = 2.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'D67N': kcat = 1.1 s-1; KM = 4.1 x 10^-4 M; printed kcat/KM = 2.7 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'D67N' (the mutant D67N entry of the single kinetic table in this article)


enzyme_display_name: XTP/dITP diphosphatase

organism: Methanocaldococcus jannaschii

substrate_name: dITP

verification_status: unverified

mutation_signature: Unknown

sequence_source: UniProtKB REST Q57679 fetched 2026-06-11

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

enzyme: XTP/dITP diphosphatase

substrate: dITP

status: unverified


substrate_name: XTP

source_db: brenda

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

proof_lines:
pH 10.5, 80°C
pH 7.6, 80°C
Raw SKiD Env: Temp=80°C, pH=10.5

source_databases_merged: brenda skid

substrate: XTP

source: brenda


organism: Thermotoga maritima

kcat_over_km_origin: calculated

sequence_source: UniProtKB REST Q9WY06 fetched 2026-06-11


substrate_name: ITP

substrate: ITP


proof_lines:
pH 9.0, 50°C
pH 9.0, 80°C
Raw SKiD Env: Temp=50°C, pH=9


organism: Trypanosoma brucei brucei

sequence_source: UniProtKB REST Q389X7 fetched 2026-06-11

proof_lines: pH 7.5, 25°C, recombinant enzyme, calculated by BRENDA


sequence_variant_note: Resolved canonical sequence from D67A reconstructed from UniProtKB REST P39304 canonical sequence fetched 2026-06-11 and applied mutation signature D67A to reconstruct the assayed variant sequence.


enzyme_display_name: diacylglycerol O-acyltransferase

organism: Brassica napus

substrate_name: oleoyl-CoA

kcat_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProt FASTA Q9M4V2; variant reconstructed from validated source mutation signature and applied mutation signature L441P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; buffer pH 7.4 assay; cofactor CoA

proof_lines: PMID 28900030 official PMC full text Table 1: BnaDGAT1 L441P Kmapp 1.31 +/- 0.10 μM for oleoyl-CoA kinetic characterization.

enzyme: diacylglycerol O-acyltransferase

substrate: oleoyl-CoA


organism: Camelina sativa

sequence_source: UniProt FASTA A0A1S6PTV7

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

proof_lines: PMC/JBC Table 2 reports CsDGAT1B wild-type K_m^app for oleoyl-CoA; row stores Km=0.00076 mM at pH 7.4 and 30°C.


sequence_variant_note: Resolved canonical sequence from UniProt FASTA A0A1S6PTV7; variant reconstructed from validated source mutation signature and applied mutation signature I466F to reconstruct the assayed variant sequence.

proof_lines: PMC/JBC Table 2 reports CsDGAT1B I466F K_m^app for oleoyl-CoA; row stores Km=0.00099 mM at pH 7.4 and 30°C.


sequence_variant_note: Resolved canonical sequence from UniProt FASTA A0A1S6PTV7; variant reconstructed from validated source mutation signature and applied mutation signature L460P/I466F to reconstruct the assayed variant sequence.

proof_lines: PMC/JBC Table 2 reports CsDGAT1B L460P/I466F K_m^app for oleoyl-CoA; row stores Km=0.0005 mM at pH 7.4 and 30°C.


sequence_variant_note: Resolved canonical sequence from UniProt FASTA A0A1S6PTV7; variant reconstructed from validated source mutation signature and applied mutation signature L460P to reconstruct the assayed variant sequence.

proof_lines: PMC/JBC Table 2 reports CsDGAT1B L460P K_m^app for oleoyl-CoA; row stores Km=0.00071 mM at pH 7.4 and 30°C.


sequence_variant_note: Resolved canonical sequence from UniProt FASTA A0A1S6PTV7; variant reconstructed from validated source mutation signature and applied mutation signature I144F to reconstruct the assayed variant sequence.

proof_lines: PMC/JBC Table 2 reports CsDGAT1B I144F K_m^app for oleoyl-CoA; row stores Km=0.00224 mM at pH 7.4 and 30°C.


organism: Homo sapiens

substrate_name: Oleoyl-CoA; sn-1,2-Dioleoylglycerol

sequence_source: UniProt FASTA Q96PD7

assay_conditions_summary: cofactor CoA

substrate: Oleoyl-CoA; sn-1,2-Dioleoylglycerol


substrate_name: palmitoleoyl-CoA

sequence_source: UniProt FASTA O75907

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

substrate: palmitoleoyl-CoA


verification_status: verified

sequence_source: UniProtKB:P39304 FASTA direct retrieval on 2026-06-11

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'wild type'; column 'kcat (s-1)' = 51; column 'KM (M)' = 6.7 x 10^-4; column 'kcat/KM (M-1 s-1)' = 7.7 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 51 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 51 s^(-1). Km: printed Table 1 cell 6.7 x 10^-4 M; 1 M is 1000 mM, so 6.7 x 10^-4 x 1000 = 0.67 mM. kcat/Km: printed Table 1 cell 7.7 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.7 x 10^4 / 1000 = 77 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'wild type': kcat = 51 s-1; KM = 6.7 x 10^-4 M; printed kcat/KM = 7.7 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'wild type' (the wild-type entry of the single kinetic table in this article)

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 FASTA direct retrieval on 2026-06-11 with E112A substitution applied after residue check and applied mutation signature E112A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant E112A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 FASTA direct retrieval on 2026-06-11 with D67N substitution applied after residue check and applied mutation signature D67N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant D67N


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'H136A'; column 'kcat (s-1)' = 2.4; column 'KM (M)' = 7.0 x 10^-4; column 'kcat/KM (M-1 s-1)' = 3.4 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.4 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 2.4 s^(-1). Km: printed Table 1 cell 7.0 x 10^-4 M; 1 M is 1000 mM, so 7.0 x 10^-4 x 1000 = 0.7 mM. kcat/Km: printed Table 1 cell 3.4 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^3 / 1000 = 3.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'H136A': kcat = 2.4 s-1; KM = 7.0 x 10^-4 M; printed kcat/KM = 3.4 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'H136A' (the mutant H136A entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature H136Q to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'H136Q'; column 'kcat (s-1)' = 1.4; column 'KM (M)' = 5.2 x 10^-4; column 'kcat/KM (M-1 s-1)' = 2.7 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.4 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 1.4 s^(-1). Km: printed Table 1 cell 5.2 x 10^-4 M; 1 M is 1000 mM, so 5.2 x 10^-4 x 1000 = 0.52 mM. kcat/Km: printed Table 1 cell 2.7 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^3 / 1000 = 2.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'H136Q': kcat = 1.4 s-1; KM = 5.2 x 10^-4 M; printed kcat/KM = 2.7 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'H136Q' (the mutant H136Q entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature E112Q/H136A/R139V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'E112Q/H136A/R139V'; column 'kcat (s-1)' = 0.2; column 'KM (M)' = 2.2 x 10^-4; column 'kcat/KM (M-1 s-1)' = 9.1 x 10^2. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.2 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.2 s^(-1). Km: printed Table 1 cell 2.2 x 10^-4 M; 1 M is 1000 mM, so 2.2 x 10^-4 x 1000 = 0.22 mM. kcat/Km: printed Table 1 cell 9.1 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.1 x 10^2 / 1000 = 0.91 s^(-1)*mM^(-1).

row_label: Table 1, printed row 'E112Q/H136A/R139V' (the mutant E112Q/H136A/R139V entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64A/R139V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64A/R139V'; column 'kcat (s-1)' = 1.2; column 'KM (M)' = 9.0 x 10^-4; column 'kcat/KM (M-1 s-1)' = 1.3 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.2 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 1.2 s^(-1). Km: printed Table 1 cell 9.0 x 10^-4 M; 1 M is 1000 mM, so 9.0 x 10^-4 x 1000 = 0.9 mM. kcat/Km: printed Table 1 cell 1.3 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^3 / 1000 = 1.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'K64A/R139V': kcat = 1.2 s-1; KM = 9.0 x 10^-4 M; printed kcat/KM = 1.3 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'K64A/R139V' (the mutant K64A/R139V entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 FASTA direct retrieval on 2026-06-11 with K64A, E112A, H136A, and R139V substitutions applied after residue checks and applied mutation signature K64A/E112A/H136A/R139V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64A/E112A/H136A/R139V


organism: Mycobacterium tuberculosis

substrate_name: diolein

sequence_source: UniProtKB canonical sequence for accession P9WKC3 (TGS4_MYCTU); direct REST lookup on 2026-06-11.

substrate: diolein


sequence_source: UniProtKB canonical sequence for accession P9WKC9 (TGS1_MYCTU); direct REST lookup on 2026-06-11.


substrate_name: palmitoyl-CoA

sequence_source: UniProtKB canonical sequence for accession P9WQP3 (A85A_MYCTU); direct REST lookup on 2026-06-11.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: palmitoyl-CoA


enzyme_display_name: protein O-GlcNAc transferase

organism: Cryptosporidium parvum

substrate_name: Protein; UDP-N-acetyl-D-glucosamine

sequence_source: UniProtKB canonical sequence for accession Q5CSU3 (Q5CSU3_CRYPI); direct REST lookup on 2026-06-11.

enzyme: protein O-GlcNAc transferase

substrate: Protein; UDP-N-acetyl-D-glucosamine


organism: Drosophila melanogaster

substrate_name: UDP-GlcNAc

sequence_source: UniProtKB canonical sequence for accession Q7KJA9 (Q7KJA9_DROME); direct REST lookup on 2026-06-11.

proof_lines: pH 7.5, temperature not specified in the publication

substrate: UDP-GlcNAc


organism: Giardia lamblia

sequence_source: UniProtKB canonical sequence for accession A8BFN4 (OGT1_GIAIC); direct REST lookup on 2026-06-11.


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

sequence_source: UniProtKB canonical sequence for accession O15294 (OGT1_HUMAN); direct REST lookup on 2026-06-11.

proof_lines: using Nup62 as cosubstrate, at 37°C, pH not specified in the publication

proof_lines: using TAB1 as cosubstrate, at 37°C, pH not specified in the publication

proof_lines: using CARM1 as cosubstrate, at 37°C, pH not specified in the publication

source_databases_merged: sabio_rk brenda skid


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

proof_lines: SABIO-RK modifier species: protein O-GlcNAc transferase(Enzyme) mutant mOGT F776A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P39304 FASTA direct check on 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature D67A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant D67A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P39304 FASTA direct check on 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature K64A/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64A/H136A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature E112Q/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'E112Q/H136A'; column 'kcat (s-1)' = 0.23; column 'KM (M)' = 1.5 x 10^-4; column 'kcat/KM (M-1 s-1)' = 1.5 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.23 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.23 s^(-1). Km: printed Table 1 cell 1.5 x 10^-4 M; 1 M is 1000 mM, so 1.5 x 10^-4 x 1000 = 0.15 mM. kcat/Km: printed Table 1 cell 1.5 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^3 / 1000 = 1.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'E112Q/H136A': kcat = 0.23 s-1; KM = 1.5 x 10^-4 M; printed kcat/KM = 1.5 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'E112Q/H136A' (the mutant E112Q/H136A entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64R/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64R/H136A'; column 'kcat (s-1)' = 4.2; column 'KM (M)' = 4.4 x 10^-4; column 'kcat/KM (M-1 s-1)' = 9.5 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.2 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 4.2 s^(-1). Km: printed Table 1 cell 4.4 x 10^-4 M; 1 M is 1000 mM, so 4.4 x 10^-4 x 1000 = 0.44 mM. kcat/Km: printed Table 1 cell 9.5 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.5 x 10^3 / 1000 = 9.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'K64R/H136A': kcat = 4.2 s-1; KM = 4.4 x 10^-4 M; printed kcat/KM = 9.5 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'K64R/H136A' (the mutant K64R/H136A entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P39304 FASTA direct check on 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature K64A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64A'; column 'kcat (s-1)' = 8.3; column 'KM (M)' = 5.1 x 10^-4; column 'kcat/KM (M-1 s-1)' = 1.6 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.3 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 8.3 s^(-1). Km: printed Table 1 cell 5.1 x 10^-4 M; 1 M is 1000 mM, so 5.1 x 10^-4 x 1000 = 0.51 mM. kcat/Km: printed Table 1 cell 1.6 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'K64A': kcat = 8.3 s-1; KM = 5.1 x 10^-4 M; printed kcat/KM = 1.6 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'K64A' (the mutant K64A entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature H136N to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'H136N'; column 'kcat (s-1)' = 4.3; column 'KM (M)' = 3.7 x 10^-4; column 'kcat/KM (M-1 s-1)' = 1.3 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.3 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 4.3 s^(-1). Km: printed Table 1 cell 3.7 x 10^-4 M; 1 M is 1000 mM, so 3.7 x 10^-4 x 1000 = 0.37 mM. kcat/Km: printed Table 1 cell 1.3 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^4 / 1000 = 13 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'H136N': kcat = 4.3 s-1; KM = 3.7 x 10^-4 M; printed kcat/KM = 1.3 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'H136N' (the mutant H136N entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P39304 FASTA direct check on 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature H136Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant H136Q


substrate_name: UDP-N-acetyl-D-glucosamine; Protein

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

proof_lines: SABIO-RK modifier species: protein O-GlcNAc transferase(Enzyme) mutant mOGT Y434A

substrate: UDP-N-acetyl-D-glucosamine; Protein


proof_lines: SABIO-RK modifier species: protein O-GlcNAc transferase(Enzyme) mutant mOGT D422A


proof_lines: SABIO-RK modifier species: protein O-GlcNAc transferase(Enzyme) mutant mOGT F752A


substrate_name: UDP-N-acetyl-D-glucosamine

sequence_source: UniProtKB:O15294 direct REST lookup on 2026-06-11

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

substrate: UDP-N-acetyl-D-glucosamine


sequence_source: UniProtKB:O15294 residues 313-1031 inclusive, direct REST lookup on 2026-06-11

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

proof_lines: SABIO-RK modifier species: protein O-GlcNAc transferase(Enzyme) mutant hOGT4.5 (residues 313-1031)


organism: Streptococcus pneumoniae TIGR4

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


proof_lines:
GtfA-GtfB complex, pH 7.5, 37°C
isolated core enzyme GtfA, pH 7.5, 37°C
Raw SKiD Env: Temp=37°C, pH=7.5


organism: Pseudomonas sp. ADP

substrate_name: ammelide

sequence_source: UniProtKB reviewed O52063 FASTA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O52063 FASTA and applied mutation signature N304A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 301.15 K; cofactor ADP

substrate: ammelide


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence reconstructed with mutation_signature E112A/H136A/R139V and applied mutation signature E112A/H136A/R139V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant E112A/H136A/R139V


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence reconstructed with mutation_signature K64A/R139V and applied mutation signature K64A/R139V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64A/R139V


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence reconstructed with mutation_signature D67A/H136A and applied mutation signature D67A/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant D67A/H136A


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence reconstructed with mutation_signature H136N and applied mutation signature H136N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant H136N


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature E112Q to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'E112Q'; column 'kcat (s-1)' = 4.0; column 'KM (M)' = 3.1 x 10^-4; column 'kcat/KM (M-1 s-1)' = 1.3 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.0 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 4 s^(-1). Km: printed Table 1 cell 3.1 x 10^-4 M; 1 M is 1000 mM, so 3.1 x 10^-4 x 1000 = 0.31 mM. kcat/Km: printed Table 1 cell 1.3 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^4 / 1000 = 13 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'E112Q': kcat = 4.0 s-1; KM = 3.1 x 10^-4 M; printed kcat/KM = 1.3 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'E112Q' (the mutant E112Q entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence reconstructed with mutation_signature E112Q/H136A and applied mutation signature E112Q/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant E112Q/H136A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature H136A/R139V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'H136A/R139V'; column 'kcat (s-1)' = 9.2; column 'KM (M)' = 1.4 x 10^-3; column 'kcat/KM (M-1 s-1)' = 6.6 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 9.2 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 9.2 s^(-1). Km: printed Table 1 cell 1.4 x 10^-3 M; 1 M is 1000 mM, so 1.4 x 10^-3 x 1000 = 1.4 mM. kcat/Km: printed Table 1 cell 6.6 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.6 x 10^3 / 1000 = 6.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'H136A/R139V': kcat = 9.2 s-1; KM = 1.4 x 10^-3 M; printed kcat/KM = 6.6 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'H136A/R139V' (the mutant H136A/R139V entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64A/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64A/H136A'; column 'kcat (s-1)' = 0.75; column 'KM (M)' = 5.8 x 10^-4; column 'kcat/KM (M-1 s-1)' = 1.3 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.75 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.75 s^(-1). Km: printed Table 1 cell 5.8 x 10^-4 M; 1 M is 1000 mM, so 5.8 x 10^-4 x 1000 = 0.58 mM. kcat/Km: printed Table 1 cell 1.3 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^3 / 1000 = 1.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'K64A/H136A': kcat = 0.75 s-1; KM = 5.8 x 10^-4 M; printed kcat/KM = 1.3 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'K64A/H136A' (the mutant K64A/H136A entry of the single kinetic table in this article)


sequence_source: UniProtKB Q57679 canonical sequence fetched by direct accession lookup on 2026-06-11.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64R to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64R'; column 'kcat (s-1)' = 17; column 'KM (M)' = 3.0 x 10^-4; column 'kcat/KM (M-1 s-1)' = 5.7 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 17 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 17 s^(-1). Km: printed Table 1 cell 3.0 x 10^-4 M; 1 M is 1000 mM, so 3.0 x 10^-4 x 1000 = 0.3 mM. kcat/Km: printed Table 1 cell 5.7 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.7 x 10^4 / 1000 = 57 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'K64R': kcat = 17 s-1; KM = 3.0 x 10^-4 M; printed kcat/KM = 5.7 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'K64R' (the mutant K64R entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P39304 canonical sequence fetched by direct accession lookup on 2026-06-11 and selected row mutation_signature H136A. and applied mutation signature H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant H136A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P39304 canonical sequence fetched by direct accession lookup on 2026-06-11 and selected row mutation_signature E112A/H136A. and applied mutation signature E112A/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant E112A/H136A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature R139V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'R139V'; column 'kcat (s-1)' = 8.9; column 'KM (M)' = 3.6 x 10^-4; column 'kcat/KM (M-1 s-1)' = 2.5 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.9 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 8.9 s^(-1). Km: printed Table 1 cell 3.6 x 10^-4 M; 1 M is 1000 mM, so 3.6 x 10^-4 x 1000 = 0.36 mM. kcat/Km: printed Table 1 cell 2.5 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^4 / 1000 = 25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'R139V': kcat = 8.9 s-1; KM = 3.6 x 10^-4 M; printed kcat/KM = 2.5 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'R139V' (the mutant R139V entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature D67A/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'D67A/H136A'; column 'kcat (s-1)' = 0.19; column 'KM (M)' = 2.7 x 10^-4; column 'kcat/KM (M-1 s-1)' = 7.0 x 10^2. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.19 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.19 s^(-1). Km: printed Table 1 cell 2.7 x 10^-4 M; 1 M is 1000 mM, so 2.7 x 10^-4 x 1000 = 0.27 mM. kcat/Km: printed Table 1 cell 7.0 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.0 x 10^2 / 1000 = 0.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'D67A/H136A': kcat = 0.19 s-1; KM = 2.7 x 10^-4 M; printed kcat/KM = 7.0 x 10^2 M-1 s-1.

row_label: Table 1, printed row 'D67A/H136A' (the mutant D67A/H136A entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature E112A/H136A/R139V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'E112A/H136A/R139V'; column 'kcat (s-1)' = 0.21; column 'KM (M)' = 7.7 x 10^-4; column 'kcat/KM (M-1 s-1)' = 2.7 x 10^2. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.21 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.21 s^(-1). Km: printed Table 1 cell 7.7 x 10^-4 M; 1 M is 1000 mM, so 7.7 x 10^-4 x 1000 = 0.77 mM. kcat/Km: printed Table 1 cell 2.7 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^2 / 1000 = 0.27 s^(-1)*mM^(-1).

row_label: Table 1, printed row 'E112A/H136A/R139V' (the mutant E112A/H136A/R139V entry of the single kinetic table in this article)


enzyme_display_name: beta-carotene 15,15'-dioxygenase

organism: uncultured marine bacterium

substrate_name: beta-carotene

sequence_source: UniProtKB reviewed accession Q4PNI0 direct lookup on 2026-06-11

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

enzyme: beta-carotene 15,15'-dioxygenase

substrate: beta-carotene


substrate_name: alpha-carotene

substrate: alpha-carotene


substrate_name: beta-apo-4'-carotenal; beta-carotene; alpha-carotene; beta-cryptoxanthin; gamma-carotene


substrate_name: gamma-carotene

substrate: gamma-carotene


enzyme_display_name: type I protein arginine methyltransferase

substrate_name: [GRGGFGGRGGFRGGRGG]-L-arginine

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

substrate: [GRGGFGGRGGFRGGRGG]-L-arginine


substrate_name: S-Adenosyl-L-methionine; GRGGFGGRGGFRGGRGG-NH2 and related peptide/protein substrates

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

sequence_source: UniProtKB reviewed accession Q99873 direct lookup on 2026-06-11

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

enzyme: type I protein arginine methyltransferase


sequence_source: UniProtKB reviewed accession O60678 direct lookup on 2026-06-11

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


organism: Gallus gallus

substrate_name: beta-cryptoxanthin

sequence_source: UniProtKB reviewed accession Q9I993 sequence version 1, direct REST check on 2026-06-11

substrate: beta-cryptoxanthin


substrate_name: O2; beta-Carotene

sequence_source: UniProtKB reviewed accession Q9HAY6 sequence version 1, direct REST check on 2026-06-11

proof_lines: recombinant enzyme, pH 7.5, temperature not specified in the publication

proof_lines: recombinant His6-tagged enzyme, pH and temperature not specified in the publication

substrate: O2; beta-Carotene


substrate_name: beta-Carotene

substrate: beta-Carotene


substrate_name: beta-Cryptoxanthin

substrate: beta-Cryptoxanthin


sequence_variant_note: Resolved canonical sequence from Q9HAY6 canonical sequence version 1 with T381L reconstructed by direct residue check on 2026-06-11 and applied mutation signature T381L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Q9HAY6 canonical sequence version 1 with K108L reconstructed by direct residue check on 2026-06-11 and applied mutation signature K108L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Q9HAY6 canonical sequence version 1 with K108F reconstructed by direct residue check on 2026-06-11 and applied mutation signature K108F to reconstruct the assayed variant sequence.


proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme


substrate_name: 3-Dehydro-L-gulonate 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature E112A/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'E112A/H136A'; column 'kcat (s-1)' = 0.45; column 'KM (M)' = 6.5 x 10^-4; column 'kcat/KM (M-1 s-1)' = 6.9 x 10^2. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.45 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.45 s^(-1). Km: printed Table 1 cell 6.5 x 10^-4 M; 1 M is 1000 mM, so 6.5 x 10^-4 x 1000 = 0.65 mM. kcat/Km: printed Table 1 cell 6.9 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.9 x 10^2 / 1000 = 0.69 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'E112A/H136A': kcat = 0.45 s-1; KM = 6.5 x 10^-4 M; printed kcat/KM = 6.9 x 10^2 M-1 s-1.

row_label: Table 1, printed row 'E112A/H136A' (the mutant E112A/H136A entry of the single kinetic table in this article)

substrate: 3-Dehydro-L-gulonate 6-phosphate


substrate_name: H+; 3-Dehydro-L-gulonate 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 REST FASTA/JSON fetched 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature H136A/R139V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant H136A/R139V

substrate: H+; 3-Dehydro-L-gulonate 6-phosphate


substrate_name: 3-Dehydro-L-gulonate 6-phosphate; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 REST FASTA/JSON fetched 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature K64R/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64R/H136A

substrate: 3-Dehydro-L-gulonate 6-phosphate; H+


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 REST FASTA/JSON fetched 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature D67N/H136A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant D67N/H136A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39304 REST FASTA/JSON fetched 2026-06-11; variant reconstructed from selected mutation_signature and applied mutation signature K64R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant K64R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature D67N/H136A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'D67N/H136A'; column 'kcat (s-1)' = 1.3; column 'KM (M)' = 3.0 x 10^-4; column 'kcat/KM (M-1 s-1)' = 4.3 x 10^3. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.3 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 1.3 s^(-1). Km: printed Table 1 cell 3.0 x 10^-4 M; 1 M is 1000 mM, so 3.0 x 10^-4 x 1000 = 0.3 mM. kcat/Km: printed Table 1 cell 4.3 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.3 x 10^3 / 1000 = 4.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'D67N/H136A': kcat = 1.3 s-1; KM = 3.0 x 10^-4 M; printed kcat/KM = 4.3 x 10^3 M-1 s-1.

row_label: Table 1, printed row 'D67N/H136A' (the mutant D67N/H136A entry of the single kinetic table in this article)


sequence_source: UniProtKB:P39304 REST FASTA/JSON fetched 2026-06-11

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'wild type'; column 'kcat (s-1)' = 51; column 'KM (M)' = 6.7 x 10^-4; column 'kcat/KM (M-1 s-1)' = 7.7 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 51 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 51 s^(-1). Km: printed Table 1 cell 6.7 x 10^-4 M; 1 M is 1000 mM, so 6.7 x 10^-4 x 1000 = 0.67 mM. kcat/Km: printed Table 1 cell 7.7 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.7 x 10^4 / 1000 = 77 s^(-1)*mM^(-1).

row_label: Table 1, printed row 'wild type' (the wild-type entry of the single kinetic table in this article)


organism: Haloferax volcanii

sequence_source: UniProtKB:D4GR06 REST FASTA/JSON fetched 2026-06-11


enzyme_display_name: thiosulfate dehydrogenase

organism: Allochromatium vinosum

substrate_name: Hexacyanoferrate(III); Thiosulfate

sequence_source: UniProtKB reviewed accession D3RVD4 direct REST/FASTA check on 2026-06-11

proof_lines:
pH 4.0, 30°C
S0.5 value, pH 4.0, 30°C
Raw SKiD Env: Temp=30°C, pH=5

enzyme: thiosulfate dehydrogenase

substrate: Hexacyanoferrate(III); Thiosulfate


substrate_name: tetrathionate

sequence_variant_note: Resolved canonical sequence from UniProtKB D3RVD4 canonical sequence plus PMID 25673691 K208N mature-chain mutation evidence and applied mutation signature K208N with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

substrate: tetrathionate


sequence_variant_note: Resolved canonical sequence from UniProtKB D3RVD4 canonical sequence plus K208N mature-chain reconstruction and applied mutation signature K208N with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant K208N, pH 5.0, 30°C, with methylviologen

proof_lines: recombinant mutant K208N, pH 5.0, 30°C, with ferricyanide

proof_lines: recombinant mutant K208N, pH 4.0, 30°C, with ferricyanide


substrate_name: thiosulfate

sequence_source: UniProtKB D3RVD4 canonical sequence plus PMID 25673691 K208N mature-chain mutation evidence

substrate: thiosulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB D3RVD4 canonical sequence plus M209G mature-chain reconstruction and applied mutation signature M209G with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant M209G, pH 5.0, 30°C, with methylviologen

proof_lines: recombinant mutant M209G, pH 5.0, 30°C, with ferricyanide

proof_lines: recombinant mutant M209G, pH 4.0, 30°C, with ferricyanide


sequence_variant_note: Resolved canonical sequence from UniProtKB D3RVD4 canonical sequence plus PMID 25673691 M209G mature-chain mutation evidence and applied mutation signature M209G with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 5.0, 30°C, with methylviologen

proof_lines: recombinant wild-type enzyme, pH 5.0, 30°C, with ferricyanide

proof_lines: recombinant wild-type enzyme, pH 4.0, 30°C, with ferricyanide


sequence_source: UniProtKB Q9NR22 reviewed entry, direct REST check 2026-06-11

unit: Mswedgeone


sequence_source: UniProtKB P55345 reviewed entry, direct REST check 2026-06-11


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

sequence_source: UniProtKB Q86X55 reviewed entry, direct REST check 2026-06-11

substrate: Unknown


substrate_name: [histone H4(1-22) peptide]-L-arginine3

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

proof_lines: recombinant enzyme mutant E153Q, pH 8.0, 30°C

substrate: [histone H4(1-22) peptide]-L-arginine3


substrate_name: [histone H4(1-16) peptide]-L-arginine3

sequence_source: UniProtKB Q99873 reviewed entry, direct REST check 2026-06-11

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

proof_lines: recombinant wild-type enzyme, pH 8.0, 30°C

substrate: [histone H4(1-16) peptide]-L-arginine3


organism: Rattus norvegicus

sequence_source: UniProtKB Q63009 reviewed entry, direct REST check 2026-06-11


substrate_name: ammelide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O52063 FASTA and applied mutation signature D303N to reconstruct the assayed variant sequence.

substrate: ammelide


assay_conditions_summary: pH 7.5; 301.15 K; buffer 200 mM sodium phosphate; cofactor ADP

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), body row 'WT'; column 'k cat (s-1)' = 26.2; column 'K M (mM)' = 3.1; column 'K cat/K M (s-1.M-1)' = 8.5 x 10^3. The uncertainty printed beside the k cat and K M cells of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 26.2 in a column headed k cat (s-1); s-1 is already the canonical s^-1, so no conversion is applied and the value is 26.2 s^(-1). Km: printed Table 2 cell 3.1 in a column headed K M (mM); mM is already canonical, so no conversion is applied and the value is 3.1 mM. kcat/Km: printed Table 2 cell 8.5 x 10^3 in a column headed K cat/K M (s-1.M-1), that is 8500 s^(-1)*M^(-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8500 / 1000 = 8.5 s^-1 mM^-1. The exported values are kcat 26.2 s^(-1), Km 3.1 mM and kcat_over_km 8.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'WT': k cat = 26.2 s-1; K M = 3.1 mM; printed K cat/K M = 8.5 x 10^3 in a column headed (s-1.M-1), that is 8500 s^(-1)*M^(-1).

row_label: Table 2, row WT

table_label: Table 2: Steady state kinetic characterization of AtzC and its variants. NDA: no detectable activity. Printed column heads: Variant; k cat (s-1); K M (mM); K cat/K M (s-1.M-1)


organism: Mus musculus

substrate_name: beta-carotene

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9JJS6 fetched by direct UniProt REST check on 2026-06-11 and applied mutation signature D52A to reconstruct the assayed variant sequence.

substrate: beta-carotene


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9JJS6 fetched by direct UniProt REST check on 2026-06-11 and applied mutation signature E140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9JJS6 fetched by direct UniProt REST check on 2026-06-11 and applied mutation signature E450A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9JJS6 fetched by direct UniProt REST check on 2026-06-11 and applied mutation signature E314A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q9JJS6 fetched by direct UniProt REST check on 2026-06-11


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9JJS6 fetched by direct UniProt REST check on 2026-06-11 and applied mutation signature H58A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q4PNI0 fetched by direct UniProt REST check on 2026-06-11


enzyme_display_name: N-acetylglucosamine kinase

organism: Shewanella sp.

substrate_name: N-Acetyl-D-glucosamine; ATP

sequence_source: UniProtKB:A0KYQ6 REST exact accession lookup on 2026-06-11

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

assay_conditions_summary: cofactor ATP

enzyme: N-acetylglucosamine kinase

substrate: N-Acetyl-D-glucosamine; ATP


substrate_name: N-Acetyl-D-glucosamine

substrate: N-Acetyl-D-glucosamine


sequence_source: UniProtKB reviewed O52063 FASTA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O52063 FASTA and applied mutation signature D188A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O52063 FASTA and applied mutation signature D188N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O52063 FASTA and applied mutation signature W309F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O52063 FASTA and applied mutation signature K65A to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:O52063 REST exact accession lookup on 2026-06-11

source: skid


substrate_name: ITP

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9BY32 REST exact accession lookup on 2026-06-11 and applied mutation signature R178C to reconstruct the assayed variant sequence.

proof_lines: pH not specified in the publication, 37°C, recombinant mutant R178C

substrate: ITP


organism: Acidithiobacillus ferrooxidans

sequence_source: UniProtKB:B7J3E3 direct lookup; AFE_0042 ordered locus in A. ferrooxidans ATCC 23270.

proof_lines:
recombinant protein, pH 2.5, 50°C
native protein, pH 2.5, 50°C


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


sequence_source: UniProtKB:D3RVD4 direct lookup; reviewed Allochromatium vinosum TsdA sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:D3RVD4 canonical precursor plus PMID 25673691 mature-protein M209G label; UniProt signal peptide is 1-27, so mature M209 maps to precursor M236. and applied mutation signature M209G with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB:D3RVD4 canonical precursor plus PMID 25673691 mature-protein K208G label; UniProt signal peptide is 1-27, so mature K208 maps to precursor K235.

sequence_variant_note: Mutation signature K208G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines: recombinant mutant K208G, pH 5.0, 30°C, with methylviologen

proof_lines: recombinant mutant K208G, pH 4.0, 30°C, with ferricyanide

proof_lines: recombinant mutant K208G, pH 5.0, 30°C, with ferricyanide


organism: Candida albicans

substrate_name: ATP; N-Acetyl-D-glucosamine

sequence_source: UniProtKB:Q59RW5 direct lookup; reviewed Candida albicans HXK1/NAG5 sequence.

substrate: ATP; N-Acetyl-D-glucosamine


organism: Saccharolobus solfataricus

substrate_name: D-glyceraldehyde

sequence_source: UniProtKB reviewed accession O54288; canonical sequence only, not row-specific mutant sequence

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

proof_lines: 70°C, pH is not specified in the publication, mutant enzyme

substrate: D-glyceraldehyde


substrate_name: pyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O54288 canonical sequence with selected-record mutation_signature applied and applied mutation signature Y103F/Y130F/A198F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y103F/Y130F/A198F, with L-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C

proof_lines: mutant enzyme Y103F/Y130F/A198F, with D-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C

proof_lines: mutant enzyme Y103F/Y130F/A198F, at pH 7.0 and 50°C

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O54288 canonical sequence with selected-record mutation_signature applied and applied mutation signature T157V/A198L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T157V/A198L, with D-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C

proof_lines: mutant enzyme T157V/A198L, with L-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C

proof_lines: mutant enzyme T157V/A198L, at pH 7.0 and 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O54288 canonical sequence with selected-record mutation_signature applied and applied mutation signature T157V/D181Q/A198L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T157V/D181Q/A198L, at pH 7.0 and 50°C

proof_lines: mutant enzyme T157V/D181Q/A198L, with D-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O54288 canonical sequence with selected-record mutation_signature applied and applied mutation signature Y132V/T157C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y132V/T157C, at pH 7.0 and 50°C

proof_lines: mutant enzyme Y132V/T157C, with D-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB reviewed accession Q4JC35 canonical sequence from direct lookup

proof_lines:
pH 6.0, 70°C
Raw SKiD Env: Temp=50°C, pH=6
Raw SKiD Env: Temp=70°C, pH=6


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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q4JC35 canonical sequence with selected-record mutation_signature applied and applied mutation signature V193A to reconstruct the assayed variant sequence.


organism: Sulfolobus solfataricus


organism: Sulfurisphaera tokodaii


enzyme_display_name: arogenate dehydratase

organism: Arabidopsis thaliana

substrate_name: L-Arogenate

enzyme: arogenate dehydratase

substrate: L-Arogenate


sequence_source: UniProtKB REST direct lookup for Q59RW5 on 2026-06-11


organism: Escherichia coli

substrate_name: ATP

sequence_source: UniProtKB REST direct lookup for P75959 on 2026-06-11

assay_conditions_summary: pH 7.6; 298.15 K; buffer a 0.3-0.5 M Tris-HCl; cofactor ATP

normalized_value_unit_evidence: YcfX / D-glucose column of Table 2: kcat 9.2 s^-1 = 9.2 s^(-1); Km,ATP 3.4 × 10-3 M = 0.0034 M = 3.4 mM (1 M = 1000 mM); kcat/Km derived 9.2 s^-1 / 3.4 mM = 2.705882352941176 s^-1 mM^-1. In the flattened text the multiplication sign renders as × and superscript exponents are flattened, so `7.6 × 10-5` is the paper's 7.6 x 10^-5, `5.4 × 106` is the paper's 5.4 x 10^6, and the unit labels `kcat (s-1)` and `kcat/Km,sugar (M-1 s-1)` are the paper's kcat (s^-1) and kcat/Km,sugar (M^-1 s^-1). Table 2 is transposed: parameters are rows and enzyme/substrate pairs are columns, in the order Glk / D-glucose, YcfX / D-glucose, NanK / D-glucose, NanK / N-acetyl-D-mannosamine, YajF / D-glucose, YajF / D-fructose.

raw_value_unit_evidence: Table 2: Kinetic Parameters for the Phosphorylation of Carbohydrates by Glk, YcfX, NanK, and YajFa | column header rows: `Glk YcfX NanK YajF` over `parameter D-glucose D-glucose D-glucose N-acetyl-D-mannosamine D-glucose D-fructose` | metric rows quoted in the captured segment: `kcat (s-1) 410 9.2 9.1 83 12 14`, `Km,sugar (M) 7.6 × 10-5 3.8 × 10-3 1.8 × 10-2 3.1 × 10-4 5.9 × 10-2 1.3 × 10-3`, `Km,ATP (M) 2.6 × 10-4 3.4 × 10-3 2.9 × 10-3 5.1 × 10-4 1.2 × 10-2 1.8 × 10-3`, `kcat/Km,sugar (M-1 s-1) 5.4 × 106 2.4 × 103 5.1 × 102 2.7 × 105 2.0 × 102 1.1 × 104` | YcfX / D-glucose column cells read: kcat = 9.2 s^-1; Km,ATP = 3.4 × 10-3 M; no kcat/Km,ATP cell is printed

row_label: YcfX | D-glucose reaction | ATP (Km,ATP)

substrate: ATP


substrate_name: D-Glucose; ATP

substrate: D-Glucose; ATP


substrate_name: D-Glucose

column_label: Table 2, YcfX column under D-glucose: kcat 9.2 s^-1; Km,sugar 3.8 × 10^-3 M = 3.8 mM; printed kcat/Km,sugar 2.4 × 10^3 M^-1 s^-1 = 2.4 s^-1 mM^-1. The current 2.4210526315789473 is the exact quotient of the first two cells and lies within the printed-efficiency rounding interval [2.35, 2.45) s^-1 mM^-1.

normalized_value_unit_evidence: The printed same-row cells normalize to kcat=9.2 s^-1 and Km=3.8 mM. Their stored-precision quotient is 9.2 / 3.8 = 2.4210526315789473 s^-1 mM^-1. The independently printed efficiency 2.4 × 10^3 M^-1 s^-1 normalizes separately to 2.4 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: kcat raw_value=9.2 raw_unit=s^-1; Km,sugar raw_value=3.8 × 10^-3 raw_unit=M; kcat/Km,sugar printed_raw_value=2.4 × 10^3 raw_unit=M^-1 s^-1

row_label: YcfX / D-glucose

table_label: Table 2: Kinetic Parameters for the Phosphorylation of Carbohydrates by Glk, YcfX, NanK, and YajF

substrate: D-Glucose


organism: Homo sapiens

sequence_source: UniProtKB REST direct lookup for Q9UJ70 on 2026-06-11


sequence_source: UniProtKB REST direct lookup for Q9QZ08 on 2026-06-11


sequence_source: UniProtKB REST direct lookup for P81799 on 2026-06-11


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY32 canonical sequence with R178A applied and applied mutation signature R178A to reconstruct the assayed variant sequence.

proof_lines: pH not specified in the publication, 37°C, recombinant mutant R178A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY32 canonical sequence with R178K applied and applied mutation signature R178K to reconstruct the assayed variant sequence.

proof_lines: pH not specified in the publication, 37°C, recombinant mutant R178K


sequence_source: UniProtKB reviewed O54288 canonical sequence


proof_lines: 60°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O54288 canonical sequence with T157C/Y132V applied and applied mutation signature T157C/Y132V to reconstruct the assayed variant sequence.

proof_lines: 70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V


proof_lines: 70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V

proof_lines: wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.0 and 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O54288 canonical sequence with T157F/Y132V applied and applied mutation signature T157F/Y132V to reconstruct the assayed variant sequence.

proof_lines: 70°C, pH is not specified in the publication, mutant enzyme T157F/Y132V


organism: Unknown


enzyme_display_name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

organism: Bos taurus

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 canonical sequence with W118F applied and applied mutation signature W118F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 canonical sequence with W118H applied and applied mutation signature W118H to reconstruct the assayed variant sequence.

enzyme: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase


sequence_source: UniProtKB Q9TTF5 canonical sequence with W118F applied


sequence_source: UniProtKB Q9TTF5 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 canonical sequence with E138A applied and applied mutation signature E138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 canonical sequence with W181A applied and applied mutation signature W181A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9TTF5 canonical sequence with W181A applied


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 canonical sequence with D147A applied and applied mutation signature D147A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature and applied mutation signature W181F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature and applied mutation signature W118A/W181A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature and applied mutation signature E138Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature and applied mutation signature E218A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature


sequence_source: UniProtKB:Q9TTF5 direct lookup

proof_lines: recombinant wild-type enzyme, pH 7.4, 37°C

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature and applied mutation signature W118H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9TTF5 direct lookup; variant reconstructed from mutation signature and applied mutation signature D147A to reconstruct the assayed variant sequence.


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed accession Q01269

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

proof_lines: enzyme purified directly from Pseudomonas aeruginosa

proof_lines: recombinant protein, purified from Escherichia coli


enzyme_display_name: cAMP-dependent protein kinase

substrate_name: Kemptide; ATP

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

enzyme: cAMP-dependent protein kinase

substrate: Kemptide; ATP


substrate_name: ATP; Kemptide

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

sequence_source: UniProt REST direct lookup P17612 / KAPCA_HUMAN on 2026-06-11

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

substrate: ATP; Kemptide


substrate_name: ATP; Sox-AKT-tide peptide

substrate: ATP; Sox-AKT-tide peptide


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


substrate_name: Kemptide

substrate: Kemptide


sequence_source: UniProt REST P17612 canonical sequence, fetched during worker review on 2026-06-11


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 canonical sequence reconstructed to R216A during worker review on 2026-06-11 and applied mutation signature R216A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 canonical sequence reconstructed to S185A during worker review on 2026-06-11 and applied mutation signature S185A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 canonical sequence reconstructed to W168A during worker review on 2026-06-11 and applied mutation signature W168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 canonical sequence reconstructed to K120A during worker review on 2026-06-11 and applied mutation signature K120A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 canonical sequence reconstructed to E138Q during worker review on 2026-06-11 and applied mutation signature E138Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 canonical sequence reconstructed to W118A during worker review on 2026-06-11 and applied mutation signature W118A to reconstruct the assayed variant sequence.


enzyme_display_name: squalene monooxygenase

substrate_name: squalene

enzyme: squalene monooxygenase

substrate: squalene


organism: Chromochloris zofingiensis

substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


enzyme_display_name: N-acylmannosamine kinase

enzyme: N-acylmannosamine kinase


enzyme_display_name: phosphoserine transaminase

enzyme: phosphoserine transaminase


enzyme_display_name: pectinesterase

organism: Malpighia glabra

substrate_name: Pectin

proof_lines:
pH 8.3, 50°C, isozyme PME2
pH 8.3, 50°C, isozyme PME1

enzyme: pectinesterase

substrate: Pectin


enzyme_display_name: bleomycin hydrolase

organism: Lactococcus lactis subsp. cremoris

sequence_source: UniProtKB reviewed entry Q04723 checked directly; row sequence reconstructed by deleting the C-terminal Ala described for the delta-Ala435 PepC mutant in PMID 9371686.

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

proof_lines: SABIO-RK modifier species: bleomycin hydrolase(Enzyme) mutant delta-Ala435

enzyme: bleomycin hydrolase


organism: Saccharomyces cerevisiae

substrate_name: H2O; L-Homocysteine thiolactone

sequence_source: UniProtKB reviewed entry Q01532 checked directly.

substrate: H2O; L-Homocysteine thiolactone


organism: Petunia x hybrida

substrate_name: L-arogenate

sequence_source: UniProtKB reviewed entry D3U715 checked directly.

substrate: L-arogenate


substrate_name: bleomycin Z

sequence_source: UniProtKB reviewed Q13867 direct REST/FASTA lookup on 2026-06-11

substrate: bleomycin Z


substrate_name: tallysomycin H1

substrate: tallysomycin H1


substrate_name: bleomycin B2

substrate: bleomycin B2


substrate_name: 6'-deoxy tallysomycin H1

substrate: 6'-deoxy tallysomycin H1


substrate_name: 6'-deoxy bleomycin Z

substrate: 6'-deoxy bleomycin Z


substrate_name: Bradykinin; H2O

mutation_type: deletion

proof_lines: SABIO-RK modifier species: bleomycin hydrolase(Enzyme) mutant PepC_Delta432-435

substrate: Bradykinin; H2O


substrate_name: H2O; Bradykinin

sequence_source: UniProtKB reviewed Q04723 direct REST/FASTA lookup on 2026-06-11

substrate: H2O; Bradykinin


enzyme_display_name: vitamin D3 24-hydroxylase

substrate_name: NADPH; H+; Calcidiol; O2

sequence_source: UniProt REST Q07973

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

enzyme: vitamin D3 24-hydroxylase

substrate: NADPH; H+; Calcidiol; O2


substrate_name: calcitriol

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

substrate: calcitriol


sequence_variant_note: Resolved canonical sequence from UniProt REST Q07973 and applied mutation signature L409S to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant L409S enzyme, pH and temperature not specified in the publication


organism: Rattus norvegicus

substrate_name: Calcidiol

sequence_source: UniProt REST Q09128

substrate: Calcidiol


substrate_name: NADPH; H+; O2; Calcidiol

assay_conditions_summary: cofactor NADP+

substrate: NADPH; H+; O2; Calcidiol


substrate_name: NAD+

sequence_source: UniProt REST Q9TTF5

sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 and applied mutation signature W118A to reconstruct the assayed variant sequence.

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9TTF5 and applied mutation signature E218Q to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant E218Q, pH 7.4, 37°C
pH 7.4, 37°C, recombinant mutant E218Q


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 FASTA retrieved 2026-06-11; W181F reconstructed after direct residue check and applied mutation signature W181F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 FASTA retrieved 2026-06-11; W118A/W181A reconstructed after direct residue checks and applied mutation signature W118A/W181A to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant W118A/W181A, pH 7.4, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 FASTA retrieved 2026-06-11; E218Q reconstructed after direct residue check and applied mutation signature E218Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9TTF5 FASTA retrieved 2026-06-11; E138A reconstructed after direct residue check and applied mutation signature E138A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9TTF5 FASTA retrieved 2026-06-11

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


sequence_source: UniProtKB Q13867 FASTA retrieved 2026-06-11


substrate_name: bleomycin A2

substrate: bleomycin A2


substrate_name: 6'-deoxy bleomycin A2

substrate: 6'-deoxy bleomycin A2


substrate_name: Pectin

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

substrate: Pectin


enzyme_display_name: sphingomyelin phosphodiesterase

substrate_name: sphingomyelin

enzyme: sphingomyelin phosphodiesterase

substrate: sphingomyelin


substrate_name: squalene

source_db: uniprot

substrate: squalene

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: calcidiol

substrate: calcidiol


enzyme_display_name: NAD(P)H oxidase (H2O2-forming)

organism: Mus musculus

substrate_name: actin (for a monooxygenase domain construct)

assay_conditions_summary: cofactor NADPH

enzyme: NAD(P)H oxidase (H2O2-forming)


organism: Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: linoleate 8R-lipoxygenase

organism: Emericella nidulans

substrate_name: palmitoleic acid

enzyme: linoleate 8R-lipoxygenase

substrate: palmitoleic acid


organism: Gaeumannomyces graminis

substrate_name: oxygen

substrate: oxygen


substrate_name: all-trans-beta-carotene (at pH 8.0 and 37 degrees Celsius)


enzyme_display_name: phenol 2-monooxygenase (NADPH)

organism: Cutaneotrichosporon cutaneum

substrate_name: phenol

enzyme: phenol 2-monooxygenase (NADPH)

substrate: phenol


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


organism: Homo sapiens

assay_conditions_summary: cofactor FAD


organism: Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4)


organism: Stutzerimonas stutzeri (strain A1501)


organism: Thiomonas intermedia (strain K12)


substrate_name: AdoMet

substrate: AdoMet


enzyme_display_name: mRNA (guanine-N(7))-methyltransferase

organism: Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)

substrate_name: N-acetyl-Gly-Arg-Arg-AMC

enzyme: mRNA (guanine-N(7))-methyltransferase

substrate: N-acetyl-Gly-Arg-Arg-AMC


organism: Kokobera virus

substrate_name: ATPase of serine protease NS3

substrate: ATPase of serine protease NS3


organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)

substrate_name: ATP

substrate: ATP


substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.4)


substrate: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.4)


enzyme_display_name: type I protein arginine methyltransferase

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


enzyme: type I protein arginine methyltransferase


substrate_name: L-homocysteine

substrate: L-homocysteine


enzyme_display_name: diacylglycerol O-acyltransferase

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

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

enzyme: diacylglycerol O-acyltransferase

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


substrate_name: retinol

substrate: retinol


enzyme_display_name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

organism: Aspergillus versicolor

substrate_name: brevianamide F

substrate: brevianamide F


enzyme_display_name: deoxyhypusine synthase

organism: Leishmania donovani

enzyme: deoxyhypusine synthase


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

substrate_name: NAD(+) (at 37 degrees Celsius when bound to regulatory subunit DHSp)


organism: Arabidopsis thaliana

substrate_name: L-glutamate

substrate: L-glutamate


organism: Niallia circulans

substrate_name: glutamate (at pH 7)

assay_conditions_summary: pH 7

substrate: glutamate (at pH 7)


enzyme_display_name: aminodeoxychorismate synthase

substrate_name: L-glutamine

enzyme: aminodeoxychorismate synthase

substrate: L-glutamine


organism: Bacillus subtilis (strain 168)

substrate_name: chorismate (with PabA and ammonia as the amino donor at pH 7.5)


organism: Escherichia coli (strain K12)

substrate_name: chorismate (with PabA and glutamine as the amino donor at pH 7.5)


substrate_name: chorismate (with the heterodimer PabA-PabB and glutamine as the amino donor at pH 7.5)


enzyme_display_name: cAMP-dependent protein kinase


enzyme_display_name: dephospho-CoA kinase

substrate_name: dephospho-CoA

enzyme: dephospho-CoA kinase

substrate: dephospho-CoA


organism: Sus scrofa

substrate_name: dephospho-CoA (in the PPAT reaction)

substrate: dephospho-CoA (in the PPAT reaction)


enzyme_display_name: triokinase

substrate_name: dihydroxyacetone

enzyme: triokinase

substrate: dihydroxyacetone


organism: Rattus norvegicus

substrate_name: FAD with manganese

substrate: FAD with manganese


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


enzyme_display_name: N-acetylglucosamine kinase

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

substrate_name: N-acetylglucosamine (GlcNAc)

enzyme: N-acetylglucosamine kinase

substrate: N-acetylglucosamine (GlcNAc)


substrate_name: GlcNAc (at 37 degrees Celsius and pH 7.5)

assay_conditions_summary: pH 7.5; cofactor ATP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: N-acetylglucosamine

substrate: N-acetylglucosamine


enzyme_display_name: GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase

substrate_name: GDP-L-galactose

substrate: GDP-L-galactose


enzyme: GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase


organism: Aquifex aeolicus (strain VF5)

substrate_name: UDP-MurNAc-pentapeptide

substrate: UDP-MurNAc-pentapeptide


enzyme_display_name: flavonol 3-sulfotransferase

organism: Flaveria chlorifolia

substrate_name: rhamnetin

enzyme: flavonol 3-sulfotransferase

substrate: rhamnetin


enzyme_display_name: pectinesterase

enzyme: pectinesterase


enzyme_display_name: histidinol-phosphatase

organism: Escherichia coli O157:H7

substrate_name: histidinol phosphate (in the presence of Mg(2+))

enzyme: histidinol-phosphatase


enzyme_display_name: sphingomyelin phosphodiesterase

organism: Caenorhabditis elegans

substrate_name: sphingomyelin (at pH 5.0)

assay_conditions_summary: pH 5

substrate: sphingomyelin (at pH 5.0)


substrate_name: sphingomyelin (N-acyl-sphing-4-enine-1-phosphocholine) (at pH 5.0)


organism: Homo sapiens

substrate_name: sphingomyelin (at pH 7.4 and 37 degrees Celsius in the presence of 0.05% Triton X-100)


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

substrate_name: NAD(+)

substrate: NAD(+)


organism: Staphylococcus aureus (strain MSSA476)

enzyme: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase


enzyme_display_name: beta-aspartyl-peptidase

substrate_name: L-asparagine (L-Asn)

enzyme: beta-aspartyl-peptidase

substrate: L-asparagine (L-Asn)


enzyme_display_name: endopeptidase La

substrate_name: ATP

enzyme: endopeptidase La

substrate: ATP


organism: Mus musculus

substrate_name: sphingomyelin (at pH 7.4 and 37 degrees Celsius)

enzyme: sphingomyelin phosphodiesterase


enzyme_display_name: alpha-D-xyloside xylohydrolase

organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)

substrate_name: isoprimeverose

enzyme: alpha-D-xyloside xylohydrolase

substrate: isoprimeverose


organism: Lactiplantibacillus pentosus


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: maltose

substrate: maltose


enzyme_display_name: beta-D-fucosidase

organism: Bifidobacterium breve

substrate_name: pNP-beta-D-glucoside

enzyme: beta-D-fucosidase

substrate: pNP-beta-D-glucoside


substrate_name: ATP for ATPase activity

substrate: ATP for ATPase activity


enzyme_display_name: chitin deacetylase

substrate_name: GlcNAc(6) (at 50 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

enzyme: chitin deacetylase


enzyme_display_name: (d)CTP diphosphatase

organism: Escherichia coli (strain K12)

enzyme: (d)CTP diphosphatase


enzyme_display_name: arogenate dehydratase

organism: Arabidopsis thaliana

substrate_name: arogenate

enzyme: arogenate dehydratase

substrate: arogenate


enzyme_display_name: mRNA (guanine-N(7))-methyltransferase

organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

enzyme: mRNA (guanine-N(7))-methyltransferase

substrate: peptide TSAVLQSGFRK-NH(2)


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


organism: Vaccinia virus (strain Western Reserve)

substrate_name: GpppA

proof_lines: A-570 and A-763 mutants have 3-fold and 10-fold higher Km values for GpppA.

substrate: GpppA


organism: Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 7.5 sec(-1) with AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:36063996). kcat is 7.7 sec(-1) for FAICAR cyclization activity (at pH 7.5 and 37 degrees Celsius) (PubMed:36063996).


substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)

proof_lines: kcat is 3.7 sec(-1) for AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:10985775). kcat is 4.1 sec(-1) for AICAR formyltransferase activity with 10-formyldihydrofolate as substrate (PubMed:10985775)


enzyme_display_name: diacylglycerol O-acyltransferase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: cofactor CoA

enzyme: diacylglycerol O-acyltransferase


enzyme_display_name: beta-carotene 15,15'-dioxygenase

substrate_name: all-trans-beta-carotene

proof_lines: kcat is 0.45 min(-1) with all-trans-beta-carotene as substrate.

enzyme: beta-carotene 15,15'-dioxygenase

substrate: all-trans-beta-carotene


organism: Uncultured marine bacterium 66A03

substrate_name: beta-carotene

proof_lines: The kcat is 4.5-fold higher with beta-carotene than with beta-cryptoxanthin as substrate.

substrate: beta-carotene


enzyme_display_name: NAD(P)H oxidase (H2O2-forming)

substrate_name: F-actin (at saturating NADPH concentration)

proof_lines: kcat is 0.28 sec(-1) for NADPH for the NADPH oxidase reaction.

enzyme: NAD(P)H oxidase (H2O2-forming)


substrate_name: NADPH

proof_lines: kcat is 11.84 min(-1) for the NADPH oxidase activity releasing hydrogen peroxide from O2.

substrate: NADPH


enzyme_display_name: type I protein arginine methyltransferase

substrate_name: S-adenosyl-L-methionine (at pH 8)

proof_lines: kcat is 0.1 min(-1) with RPS2 as substrate (at pH 8).

substrate: S-adenosyl-L-methionine (at pH 8)


organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

substrate: triphosphorylated RNA


substrate_name: C26:0-CoA (with 1,2-dipalmitin as the acyl acceptor and at 37 degrees Celsius)


enzyme_display_name: phosphoserine transaminase

proof_lines: No activity could be observed with non-phosphorylated substrates.

enzyme: phosphoserine transaminase


organism: Homo sapiens

proof_lines: kcat is 23.8 sec (-1) for the transaminase reaction with 3-phosphooxypyruvate and L-glutamate as substrates. kcat is 8.6 sec (-1) for the transaminase reaction with 2-oxoglutarate and O-phospho-L-serine as substrates.


enzyme_display_name: dephospho-CoA kinase

substrate_name: dephospho-CoA

enzyme: dephospho-CoA kinase

substrate: dephospho-CoA


enzyme_display_name: N-acetylglucosamine kinase

organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

substrate_name: N-acetylmuramate

proof_lines: kcat is 65.0 sec(-1) with GlcNAc as substrate. kcat is 42.8 sec(-1) with MurNAc as substrate.

enzyme: N-acetylglucosamine kinase

substrate: N-acetylmuramate


organism: Shewanella sp. (strain ANA-3)

substrate_name: GalNAc

proof_lines: kcat is 40.3 sec(-1) for kinase activity with GalNAc as substrate. kcat is 7.1 sec(-1) for kinase activity with GlcNAc as substrate.

substrate: GalNAc


organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

substrate_name: L-Asn

proof_lines: Enzyme is inactive on alpha-aspartyl dipeptides.

substrate: L-Asn


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)


enzyme_display_name: bleomycin hydrolase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: N-terminal acetylation of lysine-4-methyl-7-coumarylamide (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this substrate.

enzyme: bleomycin hydrolase


organism: Bombyx mori

proof_lines: kcat is 7.62 min(-1) for GlcNAc(3) (PubMed:30755482). kcat is 5.59 min(-1) for GlcNAc(4) (PubMed:30755482). kcat is 7.52 min(-1) for GlcNAc(5) (PubMed:30755482). kcat is 9.07 min(-1) for GlcNAc(6) (PubMed:30755482). kcat is 0.097 min(-1) fo


organism: Colletotrichum lindemuthianum

substrate_name: GlcNAc(2) (at 45 degrees Celsius and pH 8.5)

proof_lines: kcat is: 8.52 sec(-1) with GlcNAc(2) as substrate (at 45 degrees Celsius and pH 8.5), 11 sec(-1) with GlcNAc(2) as substrate (at 30 degrees Celsius and pH 8.5), 5.94 sec(-1) with GlcNAc(3) as substrate (at 45 degrees Celsius and pH 8.5), 1.


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

substrate_name: GlcNAc(5) (at 37 degrees Celsius, pH 8 and in presence of Co(2+))

proof_lines: kcat is 7 sec(-1) with GlcNAc(5) as substrate.


enzyme_display_name: RNA uridylyltransferase

substrate_name: UTP (at 27 degrees Celsius and with 6(U) single-stranded RNA as substrate)

proof_lines: kcat is 0.5 min(-1) with UTP (PubMed:17189640). kcat is 0.3 min(-1) with 6(U) single-stranded RNA (PubMed:17189640).

enzyme: RNA uridylyltransferase


enzyme_display_name: sphingomyelin phosphodiesterase

substrate_name: sphingomyelin

substrate: sphingomyelin


organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)

substrate_name: Xyl-alpha-PNP

proof_lines: kcat is 1.6 sec(-1) for Xyl-alpha-PNP. kcat is 0.071 sec(-1) for Glc-alpha-PNP. kcat is 32.6 sec(-1) for XXXG. kcat is 31.0 sec(-1) for XLLG. kcat is 1.78 sec(-1) for isoprimeverose.

substrate: Xyl-alpha-PNP


enzyme_display_name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

substrate_name: NAD(+)

proof_lines: kcat is 10.3 min(-1) with NAD(+) as substrate.

substrate: NAD(+)


enzyme_display_name: beta-aspartyl-peptidase

organism: Escherichia coli (strain K12)

substrate_name: beta-L-Asp-L-Leu

proof_lines: No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln, aspartylglucosamides alpha- or gamma-aspartyl dipeptides.

enzyme: beta-aspartyl-peptidase

substrate: beta-L-Asp-L-Leu


organism: Lupinus luteus

proof_lines: No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln or aspartylglucosamides.


organism: Pseudomonas sp. (strain ADP)

substrate_name: N-methylammelide

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 178 sec(-1) for N-methylammelide. kcat is 209 sec(-1) for N-ethylammelide. kcat is 80.6 sec(-1) for N-hydroxyethylammelide. kcat is 13.3 sec(-1) for N-isopropylammelide. kcat is 98.2 sec(-1) for N-cyclopropylammelide. kcat is 0.07 s

substrate: N-methylammelide


enzyme_display_name: XTP/dITP diphosphatase

substrate_name: XTP (at pH 10.0 and 37 degrees Celsius)

assay_conditions_summary: pH 10

proof_lines: Vmax values are similar for XTP, dITP and ITP. Activity toward dATP, dCTP and dTTP is less than 1% of the rate of XTP hydrolysis. dGTP and dUTP are hydrolyzed at 10-12% of the rate of XTP hydrolysis (PubMed:12297000). kcat is 5.7 sec(-1) wi

enzyme: XTP/dITP diphosphatase

substrate: XTP (at pH 10.0 and 37 degrees Celsius)


substrate_name: ITP

proof_lines: kcat is 580 sec(-1) with ITP as substrate (PubMed:11278832). kcat is 360 sec(-1) with dITP as substrate (PubMed:11278832). kcat is 640 sec(-1) with XTP as substrate (PubMed:11278832). kcat is 79.6 sec(-1) with dITP as substrate (PubMed:1709

substrate: ITP


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

substrate_name: XTP (at pH 7.6 and 80 degrees Celsius)

proof_lines: kcat is 1009 sec(-1) with XTP as substrate. kcat is 911.7 sec(-1) with ITP as substrate. kcat is 97.6 sec(-1) with GTP as substrate. kcat is 96.6 sec(-1) with dGTP as substrate (at pH 7.6 and 80 degrees Celsius) (PubMed:10404228). kcat is 1

substrate: XTP (at pH 7.6 and 80 degrees Celsius)


organism: Mus musculus

substrate_name: dITP

proof_lines: kcat is 84 sec(-1) with dITP as substrate (PubMed:17090528). kcat is 115 sec(-1) with dHAPTP as substrate (PubMed:17090528). kcat is 12.4 sec(-1) with dGTP as substrate (PubMed:17090528).

substrate: dITP


proof_lines: kcat is 33.5 sec(-1) with dITP as substrate (PubMed:17090528). kcat is 23.4 sec(-1) with dHAPTP as substrate (PubMed:17090528). kcat is 20.9 sec(-1) with dGTP as substrate (PubMed:17090528).


enzyme_display_name: N-acylmannosamine kinase

substrate_name: N-acyl-D-mannosamine (at 25 degrees Celsius and pH 7.6)

proof_lines: Catalytic efficiency with N-acyl-D-mannosamine as substrate is 136-fold higher than that with D-glucose.

enzyme: N-acylmannosamine kinase


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: UTP

proof_lines: Mutation of His-336 to Asn decreases the Km for ATP to 65 uM and increases the Km for UTP to 45 uM.

substrate: UTP


organism: Trypanosoma brucei brucei

substrate_name: UTP (with 6(U) single-stranded RNA as substrate)

proof_lines: KM is 18-28 mM for UTP (at 27 degrees Celsius and 12 (U) single-stranded RNA as substrate) (PubMed:15304317). kcat is 100 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.0012 min(-1) with UTP and dou


proof_lines: kcat is 0.18 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.04 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686).

substrate: UTP (with 6(U) single-stranded RNA as substrate)


proof_lines: kcat is 0.0007 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.002 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686). kcat is 0.02 min(-1) with UTP and with RNA with no U in 3'


substrate_name: Unknown

proof_lines: KM is 36-48 uM for UTP (at 27 degrees Celsius and with 12(U) single-stranded RNA as substrate).

substrate: Unknown


enzyme_display_name: protein O-GlcNAc transferase

organism: Arabidopsis thaliana

substrate_name: GDP-beta-L-fucose

enzyme: protein O-GlcNAc transferase

substrate: GDP-beta-L-fucose


organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6)

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Homo sapiens

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


enzyme_display_name: tryprostatin B synthase

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

substrate_name: brevianamide F

enzyme: tryprostatin B synthase

substrate: brevianamide F


enzyme_display_name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

organism: Aspergillus sp. (strain MF297-2)


enzyme_display_name: linoleate 8R-lipoxygenase

organism: Penicillium oxalicum

substrate_name: palmitoleic acid

enzyme: linoleate 8R-lipoxygenase

substrate: palmitoleic acid


enzyme_display_name: beta-carotene 15,15'-dioxygenase

organism: Galleria mellonella

substrate_name: alpha-carotene

substrate: alpha-carotene


organism: Gallus gallus

substrate_name: beta-carotene

substrate: beta-carotene


organism: Oryctolagus cuniculus

substrate_name: beta-apo-10'-carotenol + O2

substrate: beta-apo-10'-carotenol + O2


organism: Rattus norvegicus

substrate_name: all-trans-beta-carotene

sequence_source: UniProtKB reviewed accession Q91XT5 (BCDO1_RAT), exact EC 1.13.11.63 and organism Rattus norvegicus lookup

proof_lines:
pH 7.7, 37°C
intestinal enzyme

substrate: all-trans-beta-carotene


organism: Sus scrofa


enzyme_display_name: phenol 2-monooxygenase (NADPH)

organism: Acinetobacter radioresistens

substrate_name: NADH

assay_conditions_summary: cofactor NADH

enzyme: phenol 2-monooxygenase (NADPH)

substrate: NADH


organism: Auxenochlorella pyrenoidosa

substrate_name: phenol

substrate: phenol


organism: Candida albicans


organism: Candida tropicalis

substrate_name: resorcinol

proof_lines:
crude extract
at pH 7.6 and 30°C

substrate: resorcinol


organism: Cutaneotrichosporon cutaneum

proof_lines:
value depends on phenolic substrate
cosubstrate 3-fluorophenol
+ phenol or resorcinol


organism: Ectopseudomonas mendocina


organism: Pseudomonas fluorescens

proof_lines:
strain B PC18
strain F PC17
strain F PC20


organism: Pseudomonas putida

proof_lines:
strain EST1412
strain B PC30
strain B PC16


organism: Stutzerimonas stutzeri

substrate_name: Benzene

assay_conditions_summary: 298.15 K; cofactor NADPH

proof_lines:
25°C, recombinant enzyme
reconstituted enzyme complex
phenol hydrolxylase component P

substrate: Benzene


enzyme_display_name: squalene monooxygenase

organism: Homo sapiens

substrate_name: squalene

sequence_source: UniProtKB reviewed Q14534 (ERG1_HUMAN), cited to PMID 10666321

proof_lines: recombinant enzyme, Km for electron transfer partner NADPH-cytochrone P 450 reductase

enzyme: squalene monooxygenase

substrate: squalene


mutation_signature: recombinant truncated enzyme mutant

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

mutation_type: truncation

proof_lines: recombinant truncated enzyme mutant, pH 7.4, 37°C


sequence_source: UniProtKB reviewed P52020 (ERG1_RAT), cited to PMID 17112472

proof_lines: pH 7.4, 37°C, recombinant His-tagged wild-type enzyme


substrate_name: Reduced acceptor; O2; Squalene

assay_conditions_summary: pH 7.4; 310.15 K; cofactor FAD

proof_lines: non-competitive, non-time dependent inhibition

substrate: Reduced acceptor; O2; Squalene


enzyme_display_name: vitamin D3 24-hydroxylase

substrate_name: 1alpha,25-dihydroxyvitamin D3

proof_lines: wild type enzyme, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication

enzyme: vitamin D3 24-hydroxylase

substrate: 1alpha,25-dihydroxyvitamin D3


proof_lines: mutant enzyme T416S, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme T416A, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme T416V, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme I500T, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme T416M, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme I500L, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme I500F, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


substrate_name: O2; H+; Calcidiol; NADPH

proof_lines: pH and temperature not specified in the publication

substrate: O2; H+; Calcidiol; NADPH


enzyme_display_name: NAD(P)H oxidase (H2O2-forming)

organism: Bos taurus

substrate_name: Unknown

substrate: Unknown


organism: Helicobacter pylori

substrate_name: NADPH

proof_lines: at 25°C, pH not specified in the publication

substrate: NADPH


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

proof_lines: pH 7.4, 30°C, 1.5 mM Ca2+, patients with Graves disease

proof_lines: Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C


mutation_signature: N-terminal truncated recombinant enzyme N-terminal truncated recombinant enzyme


organism: Trichophyton rubrum


substrate_name: 25-hydroxyvitamin D3

proof_lines: in 0.1 mM Tris-HCl (pH 7.4), temperature not specified in the publication

substrate: 25-hydroxyvitamin D3


assay_conditions_summary: pH 7.3; 310.15 K; cofactor NADPH

proof_lines: subunit p40phox-depleted cytosol in the presence of recombinant wild-type p40phox, pH 7.3, 37°C

proof_lines: subunit p40phox-depleted cytosol in the absencee of recombinant wild-type p40phox, pH 7.3, 37°C


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 5.5; 338.15 K; cofactor NADH


assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADPH


enzyme_display_name: thiosulfate dehydrogenase

organism: Acidiphilium acidophilum

substrate_name: thiosulfate

proof_lines:
at pH 7
at least, at pH 3

enzyme: thiosulfate dehydrogenase

substrate: thiosulfate


organism: Acidithiobacillus ferrooxidans


organism: Allochromatium vinosum

substrate_name: ferricyanide

sequence_source: UniProtKB reviewed accession D3RVD4; EC 1.8.2.2 catalytic activity cites PMID 16995898.

substrate: ferricyanide


enzyme_display_name: 4-hydroxy-2-oxoheptanedioate aldolase

organism: Escherichia coli

proof_lines: The catalytic efficiency measured with 3-deoxy-D-manno-oct-2-ulosonate (KDO) is 37800-fold lower than that with 4-hydroxy-2-ketohexanoate.

enzyme: 4-hydroxy-2-oxoheptanedioate aldolase


enzyme_display_name: arogenate dehydratase

organism: Petunia hybrida

substrate_name: L-arogenate

proof_lines: kcat is 0.194 sec(-1) with L-arogenate as substrate (PubMed:20215586). kcat is 0.012 sec(-1) with prephenate as substrate (PubMed:20215586).

enzyme: arogenate dehydratase

substrate: L-arogenate


proof_lines: kcat is 0.267 sec(-1) with L-arogenate as substrate.


proof_lines: kcat is 1.231 sec(-1) with L-arogenate as substrate (PubMed:20215586). kcat is 0.060 sec(-1) with prephenate as substrate (PubMed:20215586).


organism: Campylobacter jejuni


organism: Pseudomonas aeruginosa


organism: Rhodopila globiformis


organism: Rhodotorula sp.

proof_lines: with native cytochrome c as electron acceptor


organism: Thermithiobacillus tepidarius

proof_lines:
with cytochrome c as electron acceptor
with ferricyanide as electron acceptor


enzyme_display_name: mRNA (guanine-N(7))-methyltransferase

organism: Orthopoxvirus vaccinia

substrate_name: S-adenosyl-L-methionine

proof_lines: mutant enzyme K607A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C

enzyme: mRNA (guanine-N(7))-methyltransferase

substrate: S-adenosyl-L-methionine


proof_lines: mutant enzyme F679I, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme K607R, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme F679V, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme F679L, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme N570D, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


organism: Thiobacillus sp.

proof_lines: sulfite resembles the sulfonate part of thiosulfate and might, therefore, block the active site of the enzyme

proof_lines: it is possible that selenite blocks access to the thiosulfate dehydrogenase or has an inhibiting effect on the respiratory chain itself


organism: Thiobacillus thioparus

proof_lines:
ferricyanide as electron acceptor
cytochrome c as electron acceptor


organism: Aphanothece halophytica

substrate_name: L-homocysteine; glycinebetaine

substrate: L-homocysteine; glycinebetaine


organism: Homo sapiens

substrate_name: S-methyl-L-methionine; betaine; L-homocysteine; DL-homocysteine; L-Asp

proof_lines: IC50 for betaine-homocysteine S-methyltransferase about 0.077 mM, pH 7.5, 37°C


substrate_name: betaine; L-homocysteine

sequence_variant_note: Resolved canonical sequence from UniProt Q93088 reviewed BHMT1 sequence fetched via UniProt REST; R239Q reconstructed after confirming residue 239 is R. and applied mutation signature R239Q to reconstruct the assayed variant sequence.

substrate: betaine; L-homocysteine


substrate_name: L-homocysteine; betaine

sequence_variant_note: Resolved canonical sequence from UniProt Q93088 reviewed BHMT1 sequence fetched via UniProt REST; G199S reconstructed after confirming residue 199 is G. and applied mutation signature G199S to reconstruct the assayed variant sequence.

substrate: L-homocysteine; betaine


proof_lines: mutant enzyme F679H, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: intact mRNA capping enzyme and isolated methyltransferase domain


organism: Gallus sp.


substrate_name: L-homocysteine

sequence_source: UniProtKB reviewed accession Q93088 (BHMT1_HUMAN), checked by direct UniProt FASTA/API lookup

substrate: L-homocysteine


substrate_name: betaine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q93088 with row-specific P197S substitution reconstructed during review and applied mutation signature P197S to reconstruct the assayed variant sequence.

substrate: betaine