sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G114A to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

substrate_name: UTP; N-Acetyl-D-glucosamine 1-phosphate

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_source: UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G114A

substrate: UTP; N-Acetyl-D-glucosamine 1-phosphate


substrate_name: N-Acetyl-D-glucosamine 1-phosphate; UTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G112A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G112A

substrate: N-Acetyl-D-glucosamine 1-phosphate; UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G111A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G111A


substrate_name: N-Acetyl-D-glucosamine 1-phosphate

source_db: oed

kcat_over_km_origin: calculated

source_license: CC BY 4.0

data_origin: experimental

substrate: N-Acetyl-D-glucosamine 1-phosphate

source: oed


enzyme_display_name: UDP-N-acetylglucosamine diphosphorylase

organism: Escherichia coli

substrate_name: UTP

sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; row-specific G14A variant sequence not accepted.

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

enzyme: UDP-N-acetylglucosamine diphosphorylase

substrate: UTP


mutation_signature: Unknown

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

sequence_source: UniProtKB reviewed P0ACC7 direct REST lookup.

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


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; K25A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant K25A His6-tagged


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; row-specific K25A variant sequence not accepted.


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; R18A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant R18A His6-tagged


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; deletion/truncation variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU-del78 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU-del130 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU-del227 N-terminal His6-tag


km_display: Not reported

sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; C307A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C307A N-terminal His6-tagged


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; C296A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C296A N-terminal His6-tagged


sequence_source: UniProtKB:P0ACC7 REST FASTA plus PMID 9733680 His6-GlmU C385A construct context; accessed 2026-06-07

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C385A N-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ACC7 REST FASTA plus PMID 9733680 His6-GlmU C324A construct context; accessed 2026-06-07 and applied mutation signature C324A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C324A N-terminal His6-tagged


organism: Giardia duodenalis

source_db: brenda

kcat_display: Not reported

sequence_source: UniProtKB:Q8MUP8 REST FASTA; accessed 2026-06-07

proof_lines: Mg-UTP, purified recombinant native enzyme, pH 7.5, 37°C

source: brenda


organism: Homo sapiens

sequence_source: UniProtKB:Q16222 REST FASTA; accessed 2026-06-07


organism: Mycobacterium tuberculosis

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:P9WMN3 REST FASTA; accessed 2026-06-07

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid


verification_status: corrected

sequence_source: UniProtKB:A5U161 REST FASTA; accessed 2026-06-07

assay_conditions_summary: pH 7.5; 303.15 K; buffer containing 10 mM MgCl2 throughout the purification process

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'GlcNAc-1P', fixed-substrate column value 'UTP'; column 'K_m (uM)' = 30; column 'k_cat (s^-1)' = 100; column 'k_cat/K_m (M^-1 s^-1)' = 3.2 x 10^6; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 30 uM; 30 / 1000 = 0.03 mM. kcat: printed Table 1 cell 100 s^-1; already in s^-1, no unit conversion applies, so the paper value is 100 s^(-1). kcat/Km: printed Table 1 cell 3.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.2 x 10^6 / 1000 = 3200 s^-1 mM^-1. The printed efficiency cell is the paper's own fitted catalytic efficiency and is taken as the primary reported value for this metric.

raw_value_unit_evidence: Table 1, varied-substrate row 'GlcNAc-1P', fixed substrate 'UTP': Km = 30 uM; kcat = 100 s^-1; printed kcat/Km = 3.2 x 10^6 M^-1 s^-1.

row_label: Table 1, canonical-order row with varied substrate 'GlcNAc-1P' and fixed substrate 'UTP'

table_label: Table 1: Steady-State Kinetic Parameters for GlmU (Biochemistry 2018, 57, 3387-3401)

status: corrected


verification_status: verified

assay_conditions_summary: pH 7.5; 303.15 K; buffer containing 10 mM MgCl2

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'UTP', fixed-substrate column value 'GlcNAc-1P'; column 'K_m (uM)' = 8; column 'k_cat (s^-1)' = 120; column 'k_cat/K_m (M^-1 s^-1)' = 1.5 x 10^7; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 8 uM; 8 / 1000 = 0.008 mM; the exported value is 0.008 mM. kcat: printed Table 1 cell 120 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 120.0 s^(-1). kcat/Km: printed Table 1 cell 1.5 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^7 / 1000 = 15000.0 s^-1 mM^-1; the exported value is 15000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, varied-substrate row 'UTP', fixed substrate 'GlcNAc-1P': Km = 8 uM; kcat = 120 s^-1; printed kcat/Km = 1.5 x 10^7 M^-1 s^-1.

row_label: Table 1, canonical-order row with varied substrate 'UTP' and fixed substrate 'GlcNAc-1P'

table_label: Table 1: Steady-State Kinetic Parameters for GlmU (Biochemistry 2018, 57(23):3387-3401)

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature L117A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature P122A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant P122A


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature R116A to reconstruct the assayed variant sequence.


sequence_source: uniprot:P43123 direct lookup


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature T115A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant T115A


sequence_source: uniprot:P43123 direct lookup; reconstructed from canonical sequence


substrate_name: N-acetyl-D-glucosamine 1-phosphate

substrate: N-acetyl-D-glucosamine 1-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature K123A to reconstruct the assayed variant sequence.


organism: Sulfurisphaera tokodaii

verification_status: unverified

sequence_source: UniProtKB reviewed accession Q975F9 direct REST lookup on 2026-06-07

status: unverified


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession Q975F9 direct REST lookup on 2026-06-07 with Y97N substitution and applied mutation signature Y97N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession Q975F9 direct REST lookup on 2026-06-07 with Y97V substitution and applied mutation signature Y97V to reconstruct the assayed variant sequence.


substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


substrate_name: diphosphate

substrate: diphosphate


organism: Xanthomonas oryzae pv. oryzae

substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB reviewed accession Q2P7P9 direct REST lookup on 2026-06-07

proof_lines: substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C

substrate: Unknown


enzyme_display_name: CCA tRNA nucleotidyltransferase

organism: Archaeoglobus fulgidus

substrate_name: CTP

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

sequence_source: UniProtKB reviewed accession O28126 direct REST lookup on 2026-06-07

assay_conditions_summary: pH 8.5; 323.15 K; cofactor ATP

proof_lines:
pH 8.5, 50°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=50°C, pH=8.5

source_databases_merged: brenda skid

enzyme: CCA tRNA nucleotidyltransferase

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 and applied mutation signature K123A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant K123A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 and applied mutation signature L117A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant L117A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q975F9 and applied mutation signature Y97M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q975F9 and applied mutation signature Y97V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q975F9 and applied mutation signature Y97N to reconstruct the assayed variant sequence.


organism: Exiguobacterium sibiricum

substrate_name: ATP

sequence_source: UniProtKB B1YHR1 direct REST lookup on 2026-06-07

assay_conditions_summary: pH 7.6; 277.15 K; cofactor ATP

substrate: ATP


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB Q7SIB1 direct REST lookup on 2026-06-07

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


substrate_name: a tRNA precursor

proof_lines: mutant D139A, pH not specified in the publication, temperature not specified in the publication

substrate: a tRNA precursor


sequence_source: UniProtKB Q96Q11 direct REST lookup on 2026-06-07

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


substrate_name: armless tRNA(Arg) precursor

proof_lines:
addition of 2C, pH 7.6, 20°C
addition of 2C + A, pH 7.6, 20°C

substrate: armless tRNA(Arg) precursor


organism: Methanocaldococcus jannaschii

substrate_name: tRNA precursor; ATP; CTP

sequence_source: UniProtKB Q58511 direct REST lookup on 2026-06-07

assay_conditions_summary: cofactor ATP

substrate: tRNA precursor; ATP; CTP


organism: Planococcus halocryophilus

sequence_source: UniProtKB A0A1C7DQ98 direct REST lookup on 2026-06-07

proof_lines:
pH 7.6, 25°C
pH 7.6, 4°C
Raw SKiD Env: Temp=25°C, pH=7.6


sequence_source: UniProtKB:A0A1C7DQ98 direct accession lookup


organism: Saccharolobus shibatae

sequence_source: UniProtKB:P77978 direct accession lookup


assay_conditions_summary: pH 8.1; 343.15 K; cofactor ATP


proof_lines:
pH 8.1, 70°C, wild-type enzyme
pH 9.0, 70°C, wild-type enzyme


sequence_source: UniProtKB:P77978 direct accession lookup; variant sequence not reconstructed


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature K153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature Y158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature G166R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature H129A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature G169R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature Y90E/E92F to reconstruct the assayed variant sequence.


organism: Sulfolobus shibatae

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature Y90E/E92F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant Y90E/E92F


substrate_name: CTP; ATP; tRNA precursor

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature G169R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant G169R

substrate: CTP; ATP; tRNA precursor


substrate_name: CTP; tRNA precursor; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature H129A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant H129A

substrate: CTP; tRNA precursor; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature R125A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant R125A


sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature G166R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant G166R


sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature K153A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant K153A


sequence_source: UniProtKB P77978 direct FASTA

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


substrate_name: tRNA precursor; CTP; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature H93V/Y95V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant H93V/Y95V

substrate: tRNA precursor; CTP; ATP


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


sequence_source: UniProtKB:P77978 direct FASTA, checked 2026-06-07

assay_conditions_summary: pH 9; 343.15 K; cofactor ATP

proof_lines: pH 9.0, 70°C, in presence of 0.1 mM each of UTP, ATP and GTP


sequence_source: UniProtKB:P21269 direct FASTA, checked 2026-06-07

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


proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant E92F


proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant K149A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O28126 direct REST lookup; P295T reconstructed from canonical sequence and applied mutation signature P295T to reconstruct the assayed variant sequence.

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295T

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295T

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295T


sequence_variant_note: Resolved canonical sequence from UniProtKB:O28126 direct REST lookup; P295G reconstructed from canonical sequence and applied mutation signature P295G to reconstruct the assayed variant sequence.

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295G

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295G

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295G


sequence_variant_note: Resolved canonical sequence from UniProtKB:O28126 direct REST lookup; P295A reconstructed from canonical sequence and applied mutation signature P295A to reconstruct the assayed variant sequence.

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295A

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295A

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295A


sequence_source: UniProtKB:O28126 direct REST lookup for canonical context only

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

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295SA

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295SA

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295SA


sequence_source: UniProtKB:O28126 direct REST lookup

proof_lines: A76 addition, pH and temperature not specified in the publication, wild-type enzyme

proof_lines: C74 addition, pH and temperature not specified in the publication, wild-type enzyme

proof_lines: C75 addition, pH and temperature not specified in the publication, wild-type enzyme


organism: Bacillus subtilis

sequence_source: UniProtKB:P42977 direct REST lookup


organism: Exiguobacterium artemiae

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


enzyme_display_name: guanylate kinase

substrate_name: GMP

sequence_source: UniProtKB:P60546; PMID:24722991 maps EcGK to EMBL:M84400

proof_lines: recombinant cytosolic isozyme, pH 7.5, 30°C

enzyme: guanylate kinase

substrate: GMP


enzyme_display_name: dextranase

organism: Streptococcus mutans

substrate_name: dextran T70

sequence_variant_note: Resolved canonical sequence from UniProtKB F5BA50 REST/FASTA direct check on 2026-06-07; D500T reconstructed from the checked canonical residue. and applied mutation signature D500T to reconstruct the assayed variant sequence.

enzyme: dextranase

substrate: dextran T70


substrate_name: Dextran

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB Q54443 REST/FASTA direct check on 2026-06-07.

substrate: Dextran

source: skid


organism: Pseudarthrobacter oxydans


organism: Pseudothermotoga lettingae

substrate_name: dextran T2000

sequence_source: UniProtKB:A8F6K5 direct FASTA lookup 2026-06-07

assay_conditions_summary: pH 4.3; 328.15 K; buffer 40 mM sodium acetate

proof_lines: in 40 mM sodium acetate buffer (pH4.3) at 55°C

substrate: dextran T2000


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature T563N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q54443 direct FASTA lookup 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature T558H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature W279A/T563N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W279A/T563N, at pH 5.0 and 35°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature W279F/T563N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W279F/T563N, at pH 5.0 and 35°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature W279F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P77978 reconstructed Y158A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 reconstructed Y158A and applied mutation signature Y158A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant Y158A


organism: Paenibacillus sp.


proof_lines: mutant enzyme N102C/D500G, at pH 5.0 and 40°C


proof_lines: mutant enzyme N102P/D500T, at pH 5.0 and 40°C


proof_lines: mutant enzyme N102P/D500G, at pH 5.0 and 40°C


enzyme_display_name: serine C-palmitoyltransferase

organism: Caulobacter vibrioides (strain NA1000 / CB15N)

substrate_name: hexadecanoyl-CoA

source_db: uniprot

assay_conditions_summary: cofactor CoA

enzyme: serine C-palmitoyltransferase

substrate: hexadecanoyl-CoA

source: uniprot


organism: Homo sapiens


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: GlcNAc-1-P (at pH 7.6)

assay_conditions_summary: pH 7.6; cofactor CoA

substrate: GlcNAc-1-P (at pH 7.6)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Escherichia coli (strain K12)

substrate_name: ATP (in the tRNA-NT activity assay)

substrate: ATP (in the tRNA-NT activity assay)


substrate_name: tRNA precursor

substrate: tRNA precursor


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


substrate_name: L-serine

substrate: L-serine


organism: Arabidopsis thaliana

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


substrate_name: N-acetylglucosamine 1-phosphate

substrate: N-acetylglucosamine 1-phosphate


organism: Bacteriovorax stolpii

proof_lines: kcat is 0.03 sec(-1) (in the presence of 100 uM of palmitoyl-CoA).


organism: Sphingobacterium multivorum


organism: Sphingobacterium spiritivorum


organism: Sphingomonas paucimobilis

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

proof_lines: kcat is 140 min(-1) with palmitoyl-CoA as substrate (PubMed:11279212). kcat is 2.3 sec(-1) with palmitoyl-CoA as substrate (PubMed:17557831). kcat is 1.150 sec(-1) with palmitoyl-CoA as substrate (PubMed:19376777). kcat is 0.045 sec(-1) wit


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

assay_conditions_summary: pH 7.5; 298.15 K; buffer triplicate with 10 nM hGMPK in a; cofactor NADH

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row WT; column kcat (s^-1) = 58.5 +/- 0.3; column Km (uM) = 20.7 +/- 0.3; column kcat/Km (s^-1 uM^-1) = 2.8 +/- 0.1; column s20,w (S) = 2.04 +/- 0.03; column Tm (oC) = 47.4 +/- 0.4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 58.5 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 58.5. Km: printed Table 2 cell 20.7 uM; 20.7 / 1000 = 0.0207 mM. kcat/Km: printed Table 2 cell 2.8 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.8 x 1000 = 2800.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row WT

table_label: Table 2: Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK (J. Biol. Chem. 2019, 294(31):11920-11933)


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dTMP (at pH 7.2 and 30 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 3.4 sec(-1) with dTMP as substrate (at pH 7.2 and 30 degrees Celsius) (PubMed:18477629). kcat is 3.2 sec(-1) with dTMP as substrate (at pH 7.2 and 30 degrees Celsius) (PubMed:19126267). kcat is 3.1 sec(-1) with dTMP as substrate (Pu

substrate: dTMP (at pH 7.2 and 30 degrees Celsius)


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.


organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12)

substrate_name: CTP

proof_lines: The KM for ATP is much higher than 30 uM.

substrate: CTP


organism: Bacillus licheniformis

substrate_name: Unknown

sequence: AYTVTLYLQG

wild_type_sequence: AYTVTLYLQG

proof_lines: Because of the indeterminate molecular weight of dextran, an approximate KM value of 0.3738 mg/ml was determined.

substrate: Unknown


enzyme_display_name: lignin peroxidase

organism: Agaricus bisporus

substrate_name: veratryl alcohol

enzyme: lignin peroxidase

substrate: veratryl alcohol


organism: Agaricus campestris


organism: Bjerkandera adusta

substrate_name: Veratryl alcohol; H2O2

proof_lines: lignin peroxidase activity, pH 3.5, 25°C

proof_lines: lignine peroxidas activity, pH 3.5, 25°C

substrate: Veratryl alcohol; H2O2


organism: Bjerkandera sp.

proof_lines:
Lip-2, depending on pH
Lip-5, depending on pH


organism: Brevibacillus laterosporus

substrate_name: n-Propanol

substrate: n-Propanol


organism: Comamonas sp.

substrate_name: Direct Blue GLL dye

substrate: Direct Blue GLL dye


organism: Homo sapiens

substrate_name: dGMP

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, 37ºC
pH 7.5, 30ºC
pH 7.5, isoenzyme 2

substrate: dGMP


organism: Gloeophyllum sepiarium

assay_conditions_summary: pH 2.5; 298.15 K; buffer 50 mM sodium tartrate

proof_lines: in 50 mM sodium tartrate buffer, at pH 2.5, 25°C


organism: Lentinus sajor-caju


organism: Lenzites betulinus


organism: Loweporus lividus

assay_conditions_summary: pH 2.5; 298.15 K; buffer sodium tartrate

proof_lines: 0.4 mM H2O2, 50 mM sodium tartrate buffer pH 2.5, 25°C

proof_lines: 2 mM veratryl alcohol, 50 mM sodium tartrate buffer pH 2.5, 25°C


organism: Phanerochaete chrysosporium

substrate_name: H2O2; 2,4-Dibromophenol

substrate: H2O2; 2,4-Dibromophenol


organism: Phanerodontia chrysosporium


proof_lines: pH 5.5, 30°C, purified enzyme from free Phanerochaete chrysosporium

proof_lines: pH 5.5, 30°C, purified enzyme from immobilized Phanerochaete chrysosporium


organism: Pleurotus ostreatus


organism: Pleurotus sapidus


organism: Polyporous velutinus


organism: Streptomyces griseosporeus


organism: Trametes hirsuta


organism: Trametes sanguinea


organism: Trametes versicolor

proof_lines: enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane, 25°C, pH 5.0


organism: Tropicoporus linteus


organism: Volvariella volvacea


organism: Cucurbita pepo


organism: Homo sapiens

substrate_name: myristoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines:
pH 8.0, 37°C, recombinant SPTLC3
pH 8.0, 37°C, microsomes

substrate: myristoyl-CoA


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

proof_lines: wild type protein, substrate serine, pH and temperature not specified in the publication


substrate_name: L-alanine

proof_lines: C133W mutant protein, pH not specified in the publication, temperature not specified in the publication

proof_lines: C133W mutant protein, substrate serine, pH and temperature not specified in the publication

substrate: L-alanine


organism: Rattus norvegicus


organism: Rhizorhabdus wittichii

substrate_name: stearoyl-CoA

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

substrate: stearoyl-CoA


organism: Sphingomonas paucimobilis

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 8.1; 310.15 K; cofactor CoA

proof_lines:
recombinant enzyme
native and recombinant enzyme
native enzyme

substrate: palmitoyl-CoA


organism: Bos taurus

substrate_name: GTP

proof_lines:
calculated as GDP produced
pH 7.5

substrate: GTP


organism: Helianthus tuberosus

substrate_name: GMP

substrate: GMP


assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor ATP

proof_lines: wild type enzyme, in 100 mM Tris–HCl buffer pH 7.5, 4 mM ATP, 10 mM MgCl2, 1 mM dithiothreitol, 100 mM KCl, at 30°C


proof_lines: mutant S35N/V168F, in 100 mM Tris–HCl buffer pH 7.5, 4 mM ATP, 10 mM MgCl2, 1 mM dithiothreitol, 100 mM KCl, at 30°C


organism: Mus musculus

assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
pH 8.0, 37ºC
pH 8.0, 37ºC, dGMP kinase activity


organism: Plasmodium falciparum


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from direct_uniprot_ec_organism_lookup:P15454 and applied mutation signature S35P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_ec_organism_lookup:P15454 and applied mutation signature S35P/D101S to reconstruct the assayed variant sequence.


substrate_name: ATP

assay_conditions_summary: pH 7.7; cofactor ATP

proof_lines:
pH 7.7, 25ºC, reverse reaction
pH 7.5, 25ºC
pH 7.7, 25ºC, forward reaction

substrate: ATP


sequence_variant_note: Resolved canonical sequence from direct_uniprot_ec_organism_lookup:P15454 and applied mutation signature Y78F to reconstruct the assayed variant sequence.


organism: Sus scrofa

proof_lines: pH 7.5, 30ºC, higher affinity than 9-(6-phosphonohexyl)guanine for guanylate kinases al pH values below 7.5


organism: Escherichia coli

substrate_name: N-acetyl-D-glucosamine 1-phosphate

proof_lines:
purified del227 enzyme, pH 7.4
purified del233 enzyme, pH 7.4
purified Tr250 enzyme, pH 7.4

substrate: N-acetyl-D-glucosamine 1-phosphate


organism: Giardia duodenalis

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


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


organism: Neurospora crassa


organism: Ovis aries


substrate_name: diphosphate

substrate: diphosphate


substrate_name: UTP; D-Glucose 1-phosphate

proof_lines: pH 7.5, 37°C, 10 mM N-acetyl-D-glucose 1-phosphate

substrate: UTP; D-Glucose 1-phosphate


organism: Yersinia pseudotuberculosis

proof_lines: pH 8.2, 37°C, recombinant His6-tagged enzyme


organism: Arabidopsis thaliana

substrate_name: a tRNA precursor

proof_lines: the mutant with alterations at the extreme C-terminus of the tail domain, pH 9.0, 37°C

substrate: a tRNA precursor


proof_lines: pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C74

proof_lines: pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-A76

proof_lines: pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C75


organism: Romanomermis culicivorax

substrate_name: armless tRNA(Ile) precursor

proof_lines:
addition of 2C + A, pH 7.6, 20°C
addition of 2C, pH 7.6, 20°C

substrate: armless tRNA(Ile) precursor


organism: Ascospirella lutea

substrate_name: Dextran T-2000

substrate: Dextran T-2000


organism: Aspergillus carneus

substrate_name: isomaltoheptaose

substrate: isomaltoheptaose


organism: Cellulosimicrobium sp. THN1

substrate_name: Dextran T10

substrate: Dextran T10


organism: Purpureocillium lilacinum

substrate_name: Dextran

proof_lines: isoform D-I, calculated as released reducing sugar, 40°C, pH 6.0

proof_lines: isoform D-II, calculated as released reducing sugar, 40°C, pH 5.0

proof_lines: isoform D-II, calculated as released reducing sugar, 40°C, pH 3.0

substrate: Dextran


organism: Sporothrix schenckii


organism: Streptococcus sobrinus

proof_lines:
175000-molecular-weight dextranase
160000-molecular-weight dextranase


organism: Streptomyces sp.

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


organism: Talaromyces aculeatus

proof_lines: based on the molecular weight of isomaltose


organism: Talaromyces funiculosus


organism: Talaromyces pinophilus

substrate_name: dextran T40

substrate: dextran T40


organism: Thermoanaerobacter pseudethanolicus

substrate_name: dextran T500

sequence_source: UniProtKB:B0KBZ7 (TrEMBL); RCSB PDB 5AXG accession anchor

substrate: dextran T500


organism: Chaetomium erraticum

proof_lines: ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C


organism: Chaetomium globosum

substrate_name: dextran T2000

sequence_source: UniProtKB A0A346FYQ3 / GenBank AXN77607.1

substrate: dextran T2000


organism: Fusarium verticillioides


organism: Lipomyces starkeyi


organism: Penicillium cyclopium

substrate_name: dextran T5

proof_lines:
at pH 5.0 and 50°C
at pH 5.0 and 55°C

substrate: dextran T5


organism: Polystichum aculeatum

proof_lines:
substrate dextran 40 kDa, pH 5.0, 35°C
substrate dextran 70 kDa, pH 5.0, 35°C
substrate dextran 20 kDa, pH 5.0, 35°C


organism: Plasmodium falciparum

substrate_name: dGMP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8I2M1 and RefSeq XP_001352159.1 after PMID 18374996 identified the enzyme as PlasmoDB PFI1420w; coordinate check confirmed canonical residue 76 is Y. and applied mutation signature Y76F to reconstruct the assayed variant sequence.

substrate: dGMP


substrate_name: GMP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8I2M1 and RefSeq XP_001352159.1 after PMID 18374996 identified the enzyme as PlasmoDB PFI1420w; coordinate check confirmed canonical residue 103 is N. and applied mutation signature N103D to reconstruct the assayed variant sequence.

substrate: GMP


substrate_name: Unknown

sequence_source: Canonical UniProtKB Q8I2M1 and RefSeq XP_001352159.1 sequence for the PMID 18374996 PFI1420w Plasmodium falciparum guanylate kinase family.

proof_lines:
versus ATP
versus GMP

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8I2M1 and RefSeq XP_001352159.1 after PMID 18374996 identified the enzyme as PlasmoDB PFI1420w; coordinate check confirmed canonical residue 74 is D. and applied mutation signature D74A to reconstruct the assayed variant sequence.


sequence_source: Canonical UniProtKB Q8I2M1 and RefSeq XP_001352159.1 sequence for PMID 18374996 PFI1420w Plasmodium falciparum guanylate kinase.


organism: Rattus norvegicus

substrate_name: ATP

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

substrate: ATP


enzyme_display_name: cytochrome-c peroxidase

organism: Nitrosomonas europaea

enzyme: cytochrome-c peroxidase


organism: Paracoccus denitrificans

substrate_name: ferrocytochrome c

substrate: ferrocytochrome c


organism: Paracoccus pantotrophus

substrate_name: horse heart ferrocytochrome c

assay_conditions_summary: pH 7

proof_lines: membrane solution, 50 mM NaCl, at pH 7.0

substrate: horse heart ferrocytochrome c


organism: Rhodobacter capsulatus

substrate_name: H2O2; Ferrocytochrome c2

proof_lines:
pH 7.0
horse

substrate: H2O2; Ferrocytochrome c2


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: pH 6, 20 mM potassium phosphate, wild-type enzyme

proof_lines: pH 6, 200 mM potassium phosphate, wild-type enzyme


assay_conditions_summary: pH 6

proof_lines: pH 6, 20 mM potassium phosphate, V197C/C128A mutant

proof_lines: pH 6, 200 mM potassium phosphate, V197C/C128A mutant


proof_lines: covalent complex of mutant E290C, pH 7.5, 25°C, 100 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex

proof_lines: covalent complex of mutant E290C, pH 7.5, 25°C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex


substrate_name: iso-1 ferrocytochrome c

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: Km above 0.1 mM, mutant enzyme D34K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C

substrate: iso-1 ferrocytochrome c


proof_lines: mutant enzyme E118K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


proof_lines: mutant enzyme E17K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


organism: Leishmania major

sequence_source: UniProtKB:Q4Q3K2 via RCSB 4GED

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


mutation_type: deletion

proof_lines: DELTA10 deltion mutant substrate, pH and temperature not specified in the publication


proof_lines: K98A substrate mutant, pH and temperature not specified in the publication


proof_lines: R24A substrate mutant, pH and temperature not specified in the publication


organism: Methylococcus capsulatus

substrate_name: ferrocytochrome c555

substrate: ferrocytochrome c555


organism: Geobacter sulfurreducens

sequence_source: UniProtKB Q749D0 direct accession lookup on 2026-06-07

smiles: OO


sequence_source: UniProtKB P55929 direct accession lookup on 2026-06-07


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB P14532 direct accession lookup on 2026-06-07

proof_lines: pH 7, 25 microM H2O2, protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics


substrate_name: cytochrome c

sequence_source: UniProtKB P00431 canonical accession lookup on 2026-06-07; row-specific W191 replacement not specified

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

substrate: cytochrome c


substrate_name: guaiacol

sequence_source: Reconstructed from UniProtKB P00431 canonical sequence and UniProt mature-chain feature coordinates on 2026-06-07

sequence_variant_note: Mutation signature Y36A/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: guaiacol


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P00431 canonical sequence and UniProt mature-chain feature coordinates on 2026-06-07 and applied mutation signature W191F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant W191F, pH 6.0, 25°C, the W191F mutation dramatically reduces the activity toward cytochrome c, but in the other variants which do not contain the W191F mutation the activity toward cytochrome c is largely unaffected


sequence_variant_note: Mutation signature N184R/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: ascorbate

sequence_variant_note: Mutation signature N184R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
mutant N184R, pH 6.0, 25°C
mutant FY36A/N184R, pH 6.0, 25°C

substrate: ascorbate


sequence_source: UniProtKB P00431 direct accession check; variant reconstructed from mature-chain mutation signature in selected source evidence

sequence_variant_note: Mutation signature Y36A/N184R/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant Y36A/N184R/W191F, pH 6.0, 25°C, guaiacol oxidation is not significantly affected by any of the mutations, including W191F, which is consistent with the idea that aromatic substrates such as guaiacol bind at a separate location close


sequence_source: UniProtKB P00431 direct accession check

proof_lines: wild-type cytochrome c peroxidase, pH 6.0, 25°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


substrate_name: Ferrocytochrome c; H2O2

sequence_variant_note: Mutation signature H175Q/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Gln/Trp191Phe

substrate: Ferrocytochrome c; H2O2


substrate_name: H2O2; Ferrocytochrome c

sequence_variant_note: Resolved canonical sequence from UniProtKB P00431 direct accession check; variant reconstructed from mature-chain mutation signature in selected source evidence and applied mutation signature H175Q with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Gln

substrate: H2O2; Ferrocytochrome c


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

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 P00431 direct accession check; variant reconstructed from mature-chain mutation signature in selected source evidence and applied mutation signature H175C with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Cys


sequence_variant_note: Resolved canonical sequence from uniprot:P00431|reconstructed_variant_sequence:H175E_mature_chain_maps_to_precursor_H242E and applied mutation signature H175E with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Glu


organism: Shewanella oneidensis

sequence_variant_note: Resolved canonical sequence from uniprot:Q8EF24|reconstructed_variant_sequence:F102W and applied mutation signature F102W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature D18K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D18K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E209K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E209K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E291K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E291K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E290K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E290K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E98K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E98K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature D33K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D33K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


organism: Bacillus anthracis

substrate_name: nicotinate ribonucleotide

sequence_source: RCSB:2QTR entity 1 and UniProtKB:C3L5T6 direct lookups

substrate: nicotinate ribonucleotide


organism: Escherichia coli

sequence_source: UniProtKB:P0A752 direct REST lookup, release 2026_01

assay_conditions_summary: cofactor ATP


substrate_name: beta-nicotinate D-ribonucleotide

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A752 canonical sequence using PMID 28455340 variant label; submitted A0A140NE60 is inactive/deleted and applied mutation signature Y84V/Y118D to reconstruct the assayed variant sequence.

substrate: beta-nicotinate D-ribonucleotide


sequence_source: UniProtKB:P0A752 direct REST lookup; submitted A0A140NE60 is inactive/deleted


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A752 canonical sequence using PMID 28455340 variant label; submitted A0A140NE60 is inactive/deleted and applied mutation signature A86W/Y118N to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB:P0A752 canonical sequence using PMID 28455340 variant label; submitted A0A140NE60 is inactive/deleted


enzyme_display_name: tryptophan 2,3-dioxygenase

organism: Homo sapiens

substrate_name: L-tryptophan

sequence_source: UniProtKB REST P48775 FASTA checked 2026-06-07

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

enzyme: tryptophan 2,3-dioxygenase

substrate: L-tryptophan


substrate_name: L-Tryptophan

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P48775 FASTA checked 2026-06-07 and applied mutation signature Y42A to reconstruct the assayed variant sequence.

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P48775 FASTA checked 2026-06-07 and applied mutation signature R144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P48775 FASTA checked 2026-06-07 and applied mutation signature Y45A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed P0A752 after UniProtKB A0A140NE60 direct lookup returned inactive/deleted with UniParc UPI00001120B4 mapping to P0A752. and applied mutation signature A86W/Y118N to reconstruct the assayed variant sequence.


substrate_name: reduced nicotinamide nucleotide

sequence_source: UniProtKB reviewed Q96T66 direct REST/FASTA check.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

column_label: Table 1: Kinetic Parameters of Human NMNAT Isozymes (Biochemistry 2007, volume 46, number 16, pages 4912-4922); printed substrate heads ATP, NMN, NaMN and NMNH, each with printed column heads Km (uM), kcat (s-1) and kcat/Km (s-1 M-1). Body row 'NMNAT3', substrate head 'NMNH'; column Km (uM) = 130; column kcat (s-1) = 7.2; column kcat/Km (s-1 M-1) = 0.55 x 10^5. captured primary segment: NMNAT3 | NMNH | Km 130 uM | kcat 7.2 s^-1 | kcat/Km 0.55 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 130 uM; 1 uM is 0.001 mM, so 130 / 1000 = 0.13 mM; the exported value is 0.13 mM. kcat: printed Table 1 cell 7.2 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 7.2 s^(-1); the exported value is 7.2 s^(-1). kcat/Km: printed Table 1 cell 0.55 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell is 55.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.2 / 0.13 = 55.38461538461539 s^-1 mM^-1, the exported value; in the units Table 1 prints, 7.2 s^-1 divided by 130 uM is 0.5538 x 10^5 M^-1 s^-1, which rounds to the printed catalytic-efficiency cell 0.55 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1, body row 'NMNAT3', substrate head 'NMNH': Km = 130 uM; kcat = 7.2 s^-1; printed kcat/Km = 0.55 x 10^5 M^-1 s^-1.

row_label: Table 1, body row NMNAT3, substrate head NMNH

substrate: reduced nicotinamide nucleotide


substrate_name: Nicotinate D-ribonucleotide

substrate: Nicotinate D-ribonucleotide


sequence_source: UniProtKB reviewed Q9BZQ4 direct REST/FASTA check.


substrate_name: ATP

substrate: ATP


sequence_source: UniProtKB reviewed Q9HAN9 direct REST/FASTA check.


column_label: Table 1: Kinetic Parameters of Human NMNAT Isozymes (Biochemistry 2007, volume 46, number 16, pages 4912-4922); printed substrate heads ATP, NMN, NaMN and NMNH, each with printed column heads Km (uM), kcat (s-1) and kcat/Km (s-1 M-1). Body row 'NMNAT1', substrate head 'NMNH'; column Km (uM) = 294; column kcat (s-1) = 18.6; column kcat/Km (s-1 M-1) = 0.63 x 10^5. captured primary segment: NMNAT1 | NMNH | Km 294 uM | kcat 18.6 s^-1 | kcat/Km 0.63 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 294 uM; 1 uM is 0.001 mM, so 294 / 1000 = 0.294 mM; the exported value is 0.294 mM. kcat: printed Table 1 cell 18.6 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 18.6 s^(-1); the exported value is 18.6 s^(-1). kcat/Km: printed Table 1 cell 0.63 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell is 63.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 18.6 / 0.294 = 63.26530612244899 s^-1 mM^-1, the exported value; in the units Table 1 prints, 18.6 s^-1 divided by 294 uM is 0.6327 x 10^5 M^-1 s^-1, which rounds to the printed catalytic-efficiency cell 0.63 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1, body row 'NMNAT1', substrate head 'NMNH': Km = 294 uM; kcat = 18.6 s^-1; printed kcat/Km = 0.63 x 10^5 M^-1 s^-1.

row_label: Table 1, body row NMNAT1, substrate head NMNH


substrate_name: ATP; Nicotinate D-ribonucleotide

substrate: ATP; Nicotinate D-ribonucleotide


mutation_signature: recombinant truncated enzyme mutant

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

mutation_type: truncation

proof_lines: pH 8.0, 25°C, recombinant truncated enzyme mutant


substrate_name: O2; L-Tryptophan

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant Y42A (aa 19-388)

substrate: O2; L-Tryptophan


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

proof_lines: pH and temperature not specified in the publication


substrate_name: L-Tryptophan; O2

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant TDO2 (M108I), aa 40-390, His-tagged

substrate: L-Tryptophan; O2


sequence_source: UniProtKB REST P48775 canonical sequence

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


sequence_source: UniProtKB reviewed accession Q9HAN9 direct FASTA/API lookup


sequence_source: UniProtKB reviewed accession Q96T66 direct FASTA/API lookup


sequence_source: UniProtKB reviewed accession Q9BZQ4 direct FASTA/API lookup


column_label: Table 1: Kinetic Parameters of Human NMNAT Isozymes (Biochemistry 2007, volume 46, number 16, pages 4912-4922); printed substrate heads ATP, NMN, NaMN and NMNH, each with printed column heads Km (uM), kcat (s-1) and kcat/Km (s-1 M-1). Body row 'NMNAT2', substrate head 'NMNH'; column Km (uM) = 304; column kcat (s-1) = 3.3; column kcat/Km (s-1 M-1) = 0.11 x 10^5. captured primary segment: NMNAT2 | NMNH | Km 304 uM | kcat 3.3 s^-1 | kcat/Km 0.11 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 304 uM; 1 uM is 0.001 mM, so 304 / 1000 = 0.304 mM; the exported value is 0.304 mM. kcat: printed Table 1 cell 3.3 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 3.3 s^(-1); the exported value is 3.3 s^(-1). kcat/Km: printed Table 1 cell 0.11 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell is 11.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.3 / 0.304 = 10.855263157894736 s^-1 mM^-1, the exported value; in the units Table 1 prints, 3.3 s^-1 divided by 304 uM is 0.1086 x 10^5 M^-1 s^-1, which rounds to the printed catalytic-efficiency cell 0.11 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1, body row 'NMNAT2', substrate head 'NMNH': Km = 304 uM; kcat = 3.3 s^-1; printed kcat/Km = 0.11 x 10^5 M^-1 s^-1.

row_label: Table 1, body row NMNAT2, substrate head NMNH


organism: Mycobacterium tuberculosis

substrate_name: nicotinate beta-D-ribonucleotide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJJ5 plus PMID 25631047/PDB 4RPI numbering context and applied mutation signature L164A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: nicotinate beta-D-ribonucleotide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJJ5 plus PMID 25631047/PDB 4RPI numbering context and applied mutation signature W117F with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJJ5 plus RCSB PDB 4RPI W117A construct and applied mutation signature W117A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


organism: Xanthomonas campestris

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q8PDA8_and_PMID_18783250 and applied mutation signature H55A to reconstruct the assayed variant sequence.


substrate_name: O2; 5-Fluorotryptophan

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant H55A C-terminal His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant TDO H55A, C-terminal His6-tag

substrate: O2; 5-Fluorotryptophan


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q8PDA8_and_PMID_18783250 and applied mutation signature H55S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8PDA8 direct REST/FASTA check


proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant H55S C-terminal His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant TDO H55S, C-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8PDA8 canonical sequence plus UniProt/RCSB-supported H55 variant reconstruction and applied mutation signature H55A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8PDA8 canonical sequence plus UniProt/RCSB-supported H55 variant reconstruction and applied mutation signature H55S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8PDA8 canonical sequence plus UniProt/RCSB-supported H55 variant reconstruction


smiles: O=O


organism: Monosiga brevicollis

sequence_source: UniProtKB REST direct lookup A9V766; TrEMBL; Tryptophan 2,3-dioxygenase; organism Monosiga brevicollis; EC 1.13.11.11; canonical sequence length 546.


organism: Mus musculus

sequence_source: UniProtKB REST direct lookup P48776; Swiss-Prot; Tryptophan 2,3-dioxygenase; organism Mus musculus; EC 1.13.11.11; canonical sequence length 406.


substrate_name: O2; D-Tryptophan

substrate: O2; D-Tryptophan


organism: Rattus norvegicus

sequence_source: UniProtKB REST direct lookup P21643; Swiss-Prot; Tryptophan 2,3-dioxygenase; organism Rattus norvegicus; EC 1.13.11.11; canonical sequence length 406.


sequence_source: UniProtKB REST direct lookup Q8PDA8; Swiss-Prot; Tryptophan 2,3-dioxygenase; organism Xanthomonas campestris pv. campestris strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25; EC 1.13.11.11; canonical sequence length 298.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8PDA8; direct REST FASTA/JSON check on 2026-06-07 and applied mutation signature H55S to reconstruct the assayed variant sequence.


substrate_name: 6-Methyltryptophan; O2

sequence_source: UniProtKB reviewed accession Q8PDA8; direct REST FASTA/JSON check on 2026-06-07

substrate: 6-Methyltryptophan; O2


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8PDA8; direct REST FASTA/JSON check on 2026-06-07 and applied mutation signature H55A to reconstruct the assayed variant sequence.


substrate_name: Phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08839; direct REST FASTA/JSON check on 2026-06-07 and applied mutation signature C502A to reconstruct the assayed variant sequence.

substrate: Phosphoenolpyruvate


sequence_source: UniProtKB reviewed accession P08839; direct REST FASTA/JSON check on 2026-06-07


organism: Cupriavidus metallidurans

sequence_source: UniProtKB:Q1LK00 official UniProt REST lookup 2026-06-07


sequence_source: UniProtKB:P48775 official UniProt REST lookup 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48775 official UniProt REST lookup 2026-06-07 plus selected H76S mutation signature and applied mutation signature H76S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48775 official UniProt REST lookup 2026-06-07 plus selected S151A mutation signature and applied mutation signature S151A to reconstruct the assayed variant sequence.


organism: Macaca fascicularis

sequence_source: UniProtKB:G7P6G7 official UniProt REST lookup 2026-06-07


sequence_source: UniProtKB:A9V766 official UniProt REST lookup 2026-06-07


sequence_source: UniProtKB P9WJJ5 live FASTA direct check on 2026-06-07


organism: Plasmodium falciparum

sequence_source: UniProtKB Q8IE38 live FASTA direct check on 2026-06-07

proof_lines: recombinant His6-tagged enzyme, pH 7.5, 37°C


proof_lines: mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant C43A, pH not specified in the publication, temperature not specified in the publication


substrate_name: nicotinic acid ribonucleotide

sequence_source: UniProtKB REST direct accession lookup: Q8IE38

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

substrate: nicotinic acid ribonucleotide


proof_lines: mutant C41A, pH not specified in the publication, temperature not specified in the publication


organism: Saccharomyces cerevisiae

substrate_name: diphosphate

sequence_source: UniProtKB REST direct accession lookup: P53204

substrate: diphosphate


organism: Streptococcus pyogenes

substrate_name: Unknown

sequence_source: UniProtKB REST direct accession lookup: Q5XDT7

substrate: Unknown


enzyme_display_name: adenine deaminase

organism: Aspergillus nidulans

substrate_name: H2O; Adenine

sequence_source: UniProtKB REST direct accession lookup: Q8X1T6

enzyme: adenine deaminase

substrate: H2O; Adenine


organism: Blastobotrys adeninivorans

sequence_source: UniProtKB REST direct accession lookup: L8BT48


organism: Helicobacter pylori

substrate_name: Adenine; H2O

substrate: Adenine; H2O


sequence_source: UniProtKB reviewed P9WJJ5 canonical wild-type sequence, fetched 2026-06-07

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


substrate_name: adenine

substrate: adenine


sequence_source: UniProtKB:P53909 canonical sequence; direct UniProt lookup on 2026-06-07


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB:Q9P6I7 canonical sequence; direct UniProt lookup on 2026-06-07


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


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


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Homo sapiens

substrate_name: L-tryptophan

proof_lines: kcat is 0.54 sec(-1) with L-tryptophan as substrate.

substrate: L-tryptophan


organism: Escherichia coli (strain K12)

substrate_name: mannitol phosphate

proof_lines: Enzyme I-Ntr activity requires high ionic strength.

substrate: mannitol phosphate


substrate_name: ZFPEP

proof_lines: kcat is 3830 min(-1) with PEP as substrate. kcat is 370 min(-1) with ZFPEP as substrate. kcat is 285 min(-1) with ZMePEP as substrate. kcat is 15.8 min(-1) with ZClPEP as substrate. kcat is 2.8 min(-1) with EClPEP as substrate.

substrate: ZFPEP


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

substrate_name: nicotinamide mononucleotide

proof_lines: kcat is 4.9 sec(-1) with nicotinamide mononucleotide as substrate. kcat is 3.0 sec(-1) with nicotinate mononucleotide as substrate.

substrate: nicotinamide mononucleotide


substrate_name: NMN

proof_lines: KM is >100 uM for triazofurin monophosphate.

substrate: NMN


organism: Mus musculus

substrate_name: nicotinamide mononucleotide (NMN)

proof_lines: kcat is 4.5 sec(-1) with ATP as substrate (PubMed:19403820). kcat is 5.5 sec(-1) with nicotinamide mononucleotide (NMN) as substrate (PubMed:19403820).

substrate: nicotinamide mononucleotide (NMN)


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


substrate_name: pyrogallol

proof_lines: pH 6, 20 mM potassium phosphate, covalent complex

proof_lines: pH 6, 200 mM potassium phosphate, covalent complex

substrate: pyrogallol


organism: Saccharomyces pastorianus

substrate_name: ferrocytochrome c

proof_lines: yeast, with electron acceptor ethyl peroxide

proof_lines: horse heart, with electron acceptor H2O2

substrate: ferrocytochrome c


organism: Shewanella oneidensis

proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: cytochrome c peroxidase

substrate_name: iso-1 ferrocytochrome c

sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature E201K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.100 M ionic strength potassium phosphate

proof_lines: mutant enzyme E201K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C

enzyme: cytochrome c peroxidase

substrate: iso-1 ferrocytochrome c


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature D210K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D210K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature E32K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E32K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature R31E to reconstruct the assayed variant sequence.

proof_lines: Km above 0.1 mM, mutant enzyme R31E, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature D37K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D37K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature E35K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E35K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


organism: Canis lupus

substrate_name: L-Tryptophan; O2

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

substrate: L-Tryptophan; O2


organism: Bacillus subtilis

substrate_name: deamido-NAD+

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

substrate: deamido-NAD+


organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)

substrate_name: tryptophan

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

substrate: tryptophan


organism: Staphylococcus carnosus (strain TM300)

substrate_name: PEP

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

substrate: PEP


substrate_name: beta-nicotinamide D-ribonucleotide

substrate: beta-nicotinamide D-ribonucleotide


substrate_name: ATP

substrate: ATP


organism: Escherichia coli

substrate_name: nicotinate ribonucleotide

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

substrate: nicotinate ribonucleotide


organism: Nicotiana tabacum


organism: Saccharomyces cerevisiae

proof_lines: 37°C, pH 7.5, + nicotinate ribonucleotide


organism: Alteromonas macleodii

proof_lines: pH and temperature not specified in the publication


substrate_name: adenine

sequence_source: UniProtKB reviewed accession P39761 (ADEC_BACSU), checked during EC-organism lookup

substrate: adenine


organism: Burkholderia sp.


organism: Crithidia fasciculata


sequence_source: UniProtKB:P31441; NCBI RefSeq NP_418121.1 direct lookup


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 D474N mutant label and applied mutation signature D474N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 H92Q mutant label and applied mutation signature H92Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 H92D mutant label and applied mutation signature H92D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 D285A mutant label and applied mutation signature D285A to reconstruct the assayed variant sequence.


organism: Leishmania mexicana


organism: Leishmania tarentolae


organism: Methanocaldococcus jannaschii

sequence_source: UniProt Q58854 (ADEC_METJA), reviewed EC 3.5.4.2 adenine deaminase

proof_lines: wild-type, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt Q58854 canonical sequence with C127A reconstructed after confirming residue 127 is C and applied mutation signature C127A to reconstruct the assayed variant sequence.

proof_lines: mutant C127A, pH 7.0, temperature not specified in the publication


organism: Paenarthrobacter aurescens

sequence_source: UniProt A1R3U3 (paper-linked AAur1117 / Paenarthrobacter aurescens strain TC1), unreviewed EC 3.5.4.2 entry


organism: Pseudomonas aeruginosa

sequence_source: UniProt Q9I6Y4 (ADE_PSEAE / Pseudomonas aeruginosa PAO1 Pa0148), reviewed EC 3.5.4.2 adenine deaminase


organism: Mycobacterium tuberculosis

substrate_name: nicotinate beta-D-ribonucleotide

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; W45A applied with residue-numbering offset -5 and applied mutation signature W45A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

substrate: nicotinate beta-D-ribonucleotide


sequence_source: UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; T86A applied with residue-numbering offset -5 and applied mutation signature T86A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; W45A applied with residue-numbering offset -5


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; P44A applied with residue-numbering offset -5 and applied mutation signature P44A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; K47A applied with residue-numbering offset -5 and applied mutation signature K47A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H235Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 20 mM HEPES


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H214N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature E236Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature D118N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H120N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H90N to reconstruct the assayed variant sequence.


organism: Pseudomonas synxantha

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


sequence_source: UniProtKB:P53909 reviewed entry ADE_YEAST; REST record retrieved from rest.uniprot.org.

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

assay_conditions_summary: pH 7; 306.15 K; buffer 0.2 M phosphate

proof_lines: 0.067 mM adenine in 0.2 M phosphate buffer, 33°C, pH 7.0


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB:Q9P6I7 reviewed entry ADE_SCHPO; REST record retrieved from rest.uniprot.org.


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


proof_lines: wild-type, pH 7.5, 30°C, + Fe sequestered with a metal chelator, growth medium supplemented with Mn2+ prior to induction


organism: Kluyveromyces lactis


organism: Leishmania braziliensis


organism: Leishmania donovani


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31441 and applied mutation signature H90C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

column_label: Table 3 (Catalytic constants and metal binding properties of E. coli ADE mutants), mutant row 'H90C'; column 'Km (mM)' = 0.51; column 'kcat (s^-1)' = 0.053; column 'kcat/Km (M^-1 s^-1)' = 103; column 'Metal content (Mn)' = 0.032 +/- 0.003.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.51 under the column head Km (mM); the printed millimolar column needs no conversion, so the canonical value is 0.51 mM; the exported value is 0.51 mM. kcat: printed Table 3 cell 0.053 under the column head kcat (s^-1); the printed per-second column needs no conversion, so the canonical value is 0.053 s^-1; the exported value is 0.053 s^(-1). kcat/Km: printed Table 3 cell 103 under the column head kcat/Km (M^-1 s^-1); one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 103 / 1000 = 0.103 s^-1 mM^-1; the exported value 0.10392156862745097 s^(-1)*mM^(-1) is the quotient of this row's own two printed component cells, and the printed primary cell supersedes it.

raw_value_unit_evidence: Table 3, mutant row H90C: Km = 0.51 mM (printed with its tolerance 0.51 +/- 0.05); kcat = 0.053 s^-1 (printed with its tolerance 0.053 +/- 0.008); kcat/Km = 103 M^-1 s^-1 (printed with its tolerance 103 +/- 9). The printed column heads are Km (mM), kcat (s^-1) and kcat/Km (M^-1 s^-1).

row_label: Table 3, mutant row H90C

table_label: Table 3: Catalytic constants and metal binding properties of E. coli ADE mutants (Biochemistry 2011, 50(11):1917-1927)


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature D284A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature H90Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature E185Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature H473N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature H92N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H235D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H214Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H92C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H235N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature E121Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H90D to reconstruct the assayed variant sequence.


organism: Unknown

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Streptococcus salivarius

substrate_name: histidine-containing protein

substrate: histidine-containing protein


substrate_name: Protein histidine; Phosphoenolpyruvate

proof_lines:
between 0.2 and 0.4
inhibits the phosphorylated enzyme

substrate: Protein histidine; Phosphoenolpyruvate


substrate_name: Phosphoenolpyruvate; Protein histidine

sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature C502A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate---protein phosphotransferase(Enzyme) mutant C502A

substrate: Phosphoenolpyruvate; Protein histidine


organism: Salmonella typhimurium


organism: Staphylococcus carnosus


substrate_name: protein histidine

proof_lines:
at pH 7,0
at pH 6,1
at pH 7,9

substrate: protein histidine


organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)

substrate_name: (Phosphate)(32) (at pH 8.6)

sequence_source: source_record; UniProtKB A5U654 primary-source check

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 199 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 7.5. kcat is 208 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 8.6. kcat is 108 sec(-1) with ATP as substrate at pH 7.5. kcat is 116 sec(-1) with ATP

substrate: (Phosphate)(32) (at pH 8.6)


enzyme_display_name: steroid 17alpha-monooxygenase

organism: Homo sapiens

substrate_name: progesterone (17-alpha hydroxylation)

proof_lines: kcat is 1.01 min(-1) with progesterone as substrate. kcat is 0.39 min(-1) with pregnenolone as substrate. kcat is 0.24 min(-1) with 17alpha-hydroxypregnenolone as substrate.

enzyme: steroid 17alpha-monooxygenase

substrate: progesterone (17-alpha hydroxylation)


organism: Thermobifida fusca

substrate_name: D-glucose

proof_lines: recombinant free cellulose-binding module fusion enzyme, pH 9.0, 50°C

proof_lines: recombinant free cellulose-binding module fusion enzyme, pH 7.5, 30°C

proof_lines: recombinant immobilized cellulose-binding module fusion enzyme, pH 9.0, 50°C

substrate: D-glucose


organism: Acidipropionibacterium acidipropionici


organism: Arthrobacter sp.

substrate_name: glucose

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: glucose


organism: Microlunatus phosphovorus


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.6; cofactor ATP

proof_lines:
pH 8.6
pH 7.5
pH 7.5, reaction with ATP


organism: Mycolicibacterium phlei

proof_lines:
pH 8.5, 30°C, immobilized enzyme
pH 8.5, 37°C
pH 8.5, 30°C, soluble enzyme


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: UTP

substrate: UTP


organism: Bos taurus

substrate_name: progesterone

substrate: progesterone


organism: Cavia porcellus


proof_lines:
pH 7.4
competitive substrate with progesterone
more than 0.003100


organism: Rattus norvegicus

proof_lines: C17,20 lyase activity in female duodenum


organism: Sus scrofa


substrate_name: (Phosphate)n; D-Glucose

sequence_source: UniProtKB reviewed accession A5U654

substrate: (Phosphate)n; D-Glucose


substrate_name: (Phosphate)n

substrate: (Phosphate)n


substrate_name: D-Glucose

substrate: D-Glucose


organism: Nostoc sp.

substrate_name: D-mannose

substrate: D-mannose


organism: Streptomyces coelicolor

sequence_source: UniProtKB unreviewed accession Q9ADE8

proof_lines:
at pH 7.7 and 28°C
pH 7.7, 28°C


organism: Danio rerio

proof_lines:
isoform P450 17A2, at pH 7.4 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.4


proof_lines:
isoform P450 17A1, at pH 7.4 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.4


substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 plus reconstructed R358Q and applied mutation signature R358Q to reconstruct the assayed variant sequence.

proof_lines: R358Q-mutant, inhibiton of 17alpha-hydrolase activity

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 plus reconstructed R347H and applied mutation signature R347H to reconstruct the assayed variant sequence.

proof_lines: R347H-mutant, inhibiton of 17alpha-hydrolase activity


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 plus reconstructed K89N and applied mutation signature K89N to reconstruct the assayed variant sequence.

proof_lines: K89N mutant expressed in Saccharomyces cerevisiae

proof_lines: K89N-mutant, inhibiton of 17alpha-hydrolase activity


substrate_name: NADPH; 17alpha-Hydroxyprogesterone

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

proof_lines: 17alpha-hydroxylation, pH 7.4, 37°C, presence of cytochrome b5

substrate: NADPH; 17alpha-Hydroxyprogesterone


sequence_source: UniProtKB:P05093 direct accession FASTA lookup


proof_lines: wild type, inhibiton of 17alpha-hydrolase activity


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 direct accession FASTA lookup with A105L substitution applied and applied mutation signature A105L to reconstruct the assayed variant sequence.


organism: Ovis aries

sequence_source: UniProtKB:Q29497 direct accession FASTA lookup

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

proof_lines: isozyme 1, pH 7.4, temperature not specified in the publication

proof_lines: isozyme 2, pH 7.4, temperature not specified in the publication


organism: Xenopus laevis

sequence_source: UniProtKB:Q9DDJ5 direct accession FASTA lookup


substrate_name: Pregnenolone

sequence_source: UniProtKB:Q9DDJ5 direct accession lookup

substrate: Pregnenolone


substrate_name: Progesterone

substrate: Progesterone


substrate_name: Progesterone; O2; NADPH

assay_conditions_summary: cofactor NADP+

substrate: Progesterone; O2; NADPH


organism: Anabaena sp.

substrate_name: mannose

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

substrate: mannose


organism: Corynebacterium glutamicum

substrate_name: ITP

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: pH 7.0, temperature not specified in the publication

substrate: ITP


organism: Methylomonas methanica

sequence_source: UniProtKB:A0A3G4RHV5 direct accession lookup

assay_conditions_summary: pH 8.5; 301.15 K; cofactor ATP

column_label: Retained PMC HTML Table 2, PolyP-Glk column, Glucose rows: kcat substrate 0.395 1/min; Km app 0.45 +/- 0.12 mM; kcat/Km 0.87 1/min mM.

raw_value_unit_evidence: Table 2 PolyP-Glk/Glucose cells: kcat substrate 0.395 1/min; Km app 0.45 +/- 0.12 mM; independently printed kcat/Km 0.87 1/min mM.

row_label: PolyP-Glk / Glucose

table_label: Table 2. Kinetic parameters of ATP- and polyphosphate-dependent glucokinases from Methylomonas sp. 12.


enzyme_display_name: enoyl-CoA hydratase

organism: Amycolatopsis orientalis

substrate_name: crotonyl-CoA

sequence_source: source_record; confirmed against live UniProt REST accession G4V4T7 on 2026-06-08

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) for enoyl-CoA-hydratase activity.

enzyme: enoyl-CoA hydratase

substrate: crotonyl-CoA


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)

substrate_name: crotonyl-CoA (for enoyl-CoA hydratase activity)

assay_conditions_summary: cofactor NADH


organism: Homo sapiens


substrate_name: crotonyl-CoA ((2E)-butenoyl-CoA)

substrate: crotonyl-CoA ((2E)-butenoyl-CoA)


sequence_source: UniProt REST exact accession lookup

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 canonical sequence with row-specific K242T reconstruction and applied mutation signature K242T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 canonical sequence with row-specific K242C reconstruction and applied mutation signature K242C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 canonical sequence with row-specific K242D reconstruction and applied mutation signature K242D to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis

substrate_name: crotonoyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup: P9WNP3 and applied mutation signature D40N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: crotonoyl-CoA


sequence_source: UniProtKB direct accession lookup: P9WNP3

column_label: Retained PDF journal page 2304 wild-type Rv0130 crotonoyl-CoA hydration prose: kcat 1.1 x 10^2 sec^-1; Km 55 uM; no printed kcat/Km ratio.

normalized_value_unit_evidence: Results prose: kcat 1.1 x 10^2 sec^-1 = 110 s^-1; Km 55 uM = 0.055 mM; same-measurement quotient 110 / 0.055 = 2000 s^-1 mM^-1.

raw_value_unit_evidence: Results prose: kcat 1.1 x 10^2 sec^-1. Results prose: Km 55 uM. The paper does not print a kcat/Km ratio for this measurement.

row_label: wild-type Rv0130 / crotonoyl-CoA hydration


enzyme_display_name: mannosylglycerate synthase

organism: Selaginella moellendorffii

substrate_name: GDP-alpha-D-mannose (at 50 degrees Celsius)

enzyme: mannosylglycerate synthase


organism: Rhodothermus marinus

substrate_name: D-glycerate

proof_lines: kcat is 6.5 sec(-1) for mannosylglycerate synthase activity with D-glycerate as sugar acceptor (in the presence of calcium ions at 65 degrees Celsius) (PubMed:15951819). kcat is 6.1 sec(-1) for mannosylglycerate synthase activity with GDP-M

substrate: D-glycerate


organism: Unknown


organism: Syntrophothermus lipocalidus

sequence_source: UniProtKB D7CIV8 direct REST/FASTA lookup; entry D7CIV8_SYNLT, gene Slip_2089, Syntrophothermus lipocalidus strain DSM 12680/TGB-C1.

assay_conditions_summary: pH 7.8; 338.15 K; cofactor CoA


organism: Rattus norvegicus

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

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA


proof_lines:
pH 8.0, 22°C, wild-type enzyme
pH 7.4, 25°C, wild-type enzyme


substrate_name: H2O; Crotonoyl-CoA

sequence_source: UniProtKB Q9ZPI6 canonical sequence

substrate: H2O; Crotonoyl-CoA


sequence_source: UniProtKB Q9ZPI5 canonical sequence


organism: Bos taurus

substrate_name: H2O; trans-Hex-2-enoyl-CoA

sequence_source: UniProtKB Q58DM8 canonical sequence

substrate: H2O; trans-Hex-2-enoyl-CoA


substrate_name: trans-Oct-2-enoyl-CoA; H2O

sequence_source: UniProtKB P40939 canonical sequence

substrate: trans-Oct-2-enoyl-CoA; H2O


substrate_name: Crotonoyl-CoA; H2O

sequence_source: UniProtKB Q9Y232 canonical sequence

substrate: Crotonoyl-CoA; H2O


sequence_source: UniProtKB Q08426 canonical sequence


sequence_source: UniProtKB P30084 canonical sequence


organism: Metallosphaera sedula

substrate_name: (E)-octenoyl-CoA

sequence_source: UniProtKB A4YE89 canonical sequence

substrate: (E)-octenoyl-CoA


assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

proof_lines:
pH 7.4, 25°C
25°C, ECH2
25°C, ECH1


organism: Sus scrofa

assay_conditions_summary: pH 9; cofactor CoA

proof_lines: pH 8.0, due to the binding of the enolate form of acetoacetyl-CoA the Ki-value should be highly pH-dependent


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


organism: Clostridium acetobutylicum

assay_conditions_summary: 298.15 K; cofactor CoA


organism: Escherichia coli


substrate_name: H2O; 2-Methylprop-2-enoyl-CoA

substrate: H2O; 2-Methylprop-2-enoyl-CoA


assay_conditions_summary: pH 7; 343.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProt P14604 FASTA plus PMID 10074351 Glu144Ala variant context; residue 144 in the fetched canonical sequence was directly checked as E before substitution. and applied mutation signature E144A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A4YI89 direct REST/FASTA lookup

assay_conditions_summary: pH 7.8; 315.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNP3 direct REST/FASTA lookup plus D40N reconstruction and applied mutation signature D40N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: enoyl-CoA hydratase(Enzyme) mutant D40N


sequence_source: UniProtKB:P9WNP3 direct REST/FASTA lookup


sequence_source: UniProtKB:O53561 direct REST/FASTA lookup

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: succinylated wild type enzyme, at pH 7.4, temperature not specified in the publication


organism: Nitrosopumilus maritimus

sequence_source: UniProtKB:A9A2G5 direct REST/FASTA lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 direct REST/FASTA lookup plus K242T reconstruction and applied mutation signature K242T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: enoyl-CoA hydratase(Enzyme) mutant K242T (His-tagged)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 direct REST/FASTA lookup plus K242C reconstruction and applied mutation signature K242C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: enoyl-CoA hydratase(Enzyme) mutant K242C (His-tagged)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 direct REST/FASTA lookup plus K242D reconstruction and applied mutation signature K242D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: enoyl-CoA hydratase(Enzyme) mutant K242D (His-tagged)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature T139A to reconstruct the assayed variant sequence.

proof_lines: mutant T139A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature W189A to reconstruct the assayed variant sequence.

proof_lines: mutant W189A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature E166A to reconstruct the assayed variant sequence.

proof_lines: mutant E166A, pH 7.0, 23°C, presence of Mn2+


substrate_name: D-lactate

sequence_source: UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present.

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

proof_lines: wild-type, pH 7.0, 23°C, presence of Mn2+

proof_lines: wild-type, pH 7.0, 23°C, presence of 3 mM Ca2+

proof_lines: wild-type, pH 7.0, 23°C, presence of 3 mM Mg2+

substrate: D-lactate


substrate_name: GDP-mannose

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature R73A to reconstruct the assayed variant sequence.

proof_lines: mutant R73A, pH 7.0, 23°C, presence of Mn2+

substrate: GDP-mannose


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature M229A to reconstruct the assayed variant sequence.

proof_lines: mutant M229A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature Y220F to reconstruct the assayed variant sequence.

proof_lines: mutant Y220F, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RFR0; variant sequence reconstructed from the checked canonical sequence when mutation_signature is present. and applied mutation signature Y220A to reconstruct the assayed variant sequence.

proof_lines: mutant Y220A, pH 7.0, 23°C, presence of Mn2+


substrate_name: GDP-glucose

sequence_source: UniProtKB Q9RFR0 direct EC+organism lookup; PubMed PMID 15951819 and RCSB 2BO4 support the Rhodothermus marinus MGS identity.

proof_lines:
pH 7.8, 25°C, cosubstrate: D-glycerate
pH 7.8, 65°C, cosubstrate: GDP-mannose
pH 7.8, 65°C, cosubstrate: D-glycerate

substrate: GDP-glucose


sequence_source: UniProtKB D8S5L4 direct EC+organism lookup; PubMed PMID 23179444 supports the Selaginella moellendorffii MgS identity.

proof_lines:
pH 8.0, 25°C
pH 8.0, 50°C
cosubstrate GDP-mannose, pH 8.0, 25°C


substrate_name: GDPmannose; D-Glycerate

proof_lines:
pH 7.6, 90°C, recombinant enzyme
pH 7.6, 90°C, native enzyme
Raw SKiD Env: Temp=23°C, pH=7

substrate: GDPmannose; D-Glycerate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature Q66A to reconstruct the assayed variant sequence.

proof_lines: mutant Q66A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature K9A to reconstruct the assayed variant sequence.

proof_lines: mutant K9A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature H217A to reconstruct the assayed variant sequence.

proof_lines: mutant H217A, pH 7.0, 23°C, presence of Mn2+

proof_lines: mutant H217A, pH 7.0, 23°C, presence of 3 mM Mg2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature K76A to reconstruct the assayed variant sequence.

proof_lines: mutant K76A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature D135A to reconstruct the assayed variant sequence.

proof_lines: mutant D135A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature R218A to reconstruct the assayed variant sequence.

proof_lines: mutant R218A, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RFR0 and applied mutation signature R73G to reconstruct the assayed variant sequence.

proof_lines: mutant R73G, pH 7.0, 23°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9RFR0 canonical sequence with Y37A row-specific reconstruction from the selected BRENDA note and applied mutation signature Y37A to reconstruct the assayed variant sequence.

proof_lines: mutant Y37A, pH 7.0, 23°C, presence of Mn2+


enzyme_display_name: plasmin

sequence_source: UniProtKB reviewed P00747 canonical sequence from direct accession lookup

enzyme: plasmin


sequence_source: UniProtKB reviewed P06867 canonical sequence from direct accession lookup


enzyme_display_name: acylglycerol lipase

substrate_name: monoacylglycerol

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

enzyme: acylglycerol lipase

substrate: monoacylglycerol


substrate_name: lysophosphatidylethanolamine

proof_lines:
pH 8.0, 30°C, AtMAGL4
pH 8.0, 30°C, AtMAGL2

substrate: lysophosphatidylethanolamine