organism: Mycobacterium tuberculosis

substrate_name: Guanosine 3',5'-bis(diphosphate)

sequence_source: UniProt REST direct lookup P9WHG9

substrate: Guanosine 3',5'-bis(diphosphate)


source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

status: unverified

source: oed


enzyme_display_name: yapsin 1

organism: Saccharomyces cerevisiae

substrate_name: amidorphin

sequence_source: UniProt REST direct lookup P32329

enzyme: yapsin 1

substrate: amidorphin


substrate_name: Adrenocorticotropic hormone 1-39; H2O

kcat_over_km_display: Not reported

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

substrate: Adrenocorticotropic hormone 1-39; H2O


substrate_name: Dynorphin B (1-13)

substrate: Dynorphin B (1-13)


substrate_name: Dynorphin A (1-11)

substrate: Dynorphin A (1-11)


organism: Escherichia coli

substrate_name: succinyl-CoA

source_db: brenda

kcat_display: Not reported

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

assay_conditions_summary: cofactor CoA

proof_lines:
vs. L-2-aminopimelate
vs. tetrahydropicolinate

substrate: succinyl-CoA

source: brenda


organism: Pseudomonas aeruginosa


substrate_name: dihydroxyacetone

substrate: dihydroxyacetone


substrate_name: Proinsulin

substrate: Proinsulin


enzyme_display_name: Anthranilate O-methyltransferase 1

organism: Zea mays

substrate_name: anthranilate

sequence_source: UniProtKB reviewed accession D9J0Z7; matching NCBI protein ADI87449.1 translated from GenBank HM242244.1

proof_lines: 25°C, pH not specified in the publication, isoenzyme AAMT1

enzyme: Anthranilate O-methyltransferase 1

substrate: anthranilate


enzyme_display_name: cyanamide hydratase

organism: Albifimbria verrucaria

substrate_name: cyanamide

sequence_source: UniProtKB P22143 / CYAH_ALBVE exact EC+organism lookup; UniProt release 2026_02 reported X-Total-Results: 1 for organism_name:"Albifimbria verrucaria" AND ec:4.2.1.69.

smiles: C(#N)N

enzyme: cyanamide hydratase

substrate: cyanamide


enzyme_display_name: anthranilate O-methyltransferase

substrate_name: S-adenosyl-L-methionine

source_db: uniprot

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

enzyme: anthranilate O-methyltransferase

substrate: S-adenosyl-L-methionine

source: uniprot


organism: Homo sapiens


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: (S)-ureidoglycine aminohydrolase

organism: Arabidopsis thaliana

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProt direct lookup Q8GXV5

enzyme: (S)-ureidoglycine aminohydrolase

source: skid


organism: Myrothecium verrucaria

substrate_name: Cyanamide

sequence_source: UniProt direct lookup P22143

smiles: N=C=N

substrate: Cyanamide


substrate_name: H2O; Cyanamide

substrate: H2O; Cyanamide


sequence_source: UniProt direct lookup P0CH63


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P0CH63 canonical sequence and H137N mutation signature and applied mutation signature H137N to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P0CH63 canonical sequence and T157V mutation signature and applied mutation signature T157V to reconstruct the assayed variant sequence.


enzyme_display_name: L-arginine hydroxylase

organism: Streptomyces vinaceus

substrate_name: L-arginine

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

sequence_source: UniProtKB Q6WZB0 direct REST lookup; sequence matched

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8

source_databases_merged: brenda skid

enzyme: L-arginine hydroxylase

substrate: L-arginine


substrate_name: L-homoarginine

substrate: L-homoarginine


substrate_name: L-Arginine

substrate: L-Arginine


substrate_name: L-canavanine

substrate: L-canavanine


substrate_name: Anthranilate; S-Adenosyl-L-methionine

sequence_source: UniProtKB D9J0Z7 direct REST lookup; sequence matched

substrate: Anthranilate; S-Adenosyl-L-methionine


substrate_name: Anthranilate

substrate: Anthranilate


substrate_name: S-Adenosyl-L-methionine; Anthranilate

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

sequence_source: UniProtKB B6SU46 direct REST lookup; sequence matched

proof_lines: 25°C, pH not specified in the publication, isoenzyme AAMT2

substrate: S-Adenosyl-L-methionine; Anthranilate


sequence_source: UniProtKB D9J100 direct REST lookup; sequence matched

proof_lines: 25°C, pH not specified in the publication, isoenzyme AAMT3


substrate_name: benzoate

substrate: benzoate


sequence_source: UniProtKB Q8GXV5 direct REST lookup; sequence matched


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8GXV5 direct REST lookup; sequence matched and applied mutation signature K291R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8GXV5 direct REST lookup; sequence matched and applied mutation signature Y252F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P46959, sequenceVersion 1, direct REST FASTA/JSON lookup

proof_lines: pH 8.0, 30°C, purified FlagGcd10pyGcd14p complex


organism: Thermus thermophilus

substrate_name: S-Adenosyl-L-methionine; tRNA

sequence_source: UniProtKB reviewed accession Q8GBB2, sequenceVersion 2, direct REST FASTA/JSON lookup

substrate: S-Adenosyl-L-methionine; tRNA


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GBB2 canonical sequence with D170A reconstructed after direct residue check and applied mutation signature D170A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (adenine58-N1)-methyltransferase(Enzyme) mutant D170A N-terminal His6-tag


substrate_name: tRNA; S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GBB2 canonical sequence with Y78A reconstructed after direct residue check and applied mutation signature Y78A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (adenine58-N1)-methyltransferase(Enzyme) mutant Y78A N-terminal His6-tag

substrate: tRNA; S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GBB2 canonical sequence with Y194A reconstructed after direct residue check and applied mutation signature Y194A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (adenine58-N1)-methyltransferase(Enzyme) mutant Y194A N-terminal His6-tag


substrate_name: adenine58 in tRNAPhe

proof_lines: pH 7.5-8.0, 55°C, wild-type Thermus thermophilus tRNAPhe as substrate

substrate: adenine58 in tRNAPhe


substrate_name: L-canavanine (at pH 8 and 30 degrees Celsius)

assay_conditions_summary: pH 8

proof_lines: kcat is 2611 min(-1), 831 min(-1) and 73.2 min(-1) for L-arginine, L-homoarginine and L-canavanine, respectively (at pH 8 and 30 degrees Celsius).


substrate_name: anthranilic acid

proof_lines: kcat is 0.37 sec(-1) with anthranilic acid as substrate.

substrate: anthranilic acid


proof_lines: kcat is 0.45 sec(-1) with anthranilic acid as substrate. kcat is 0.04 sec(-1) with benzoic acid as substrate.


verification_status: corrected

assay_conditions_summary: cofactor NADH

proof_lines: kcat is 761 sec(-1) for (S)-2-ureidoglycine.

status: corrected


enzyme_display_name: carotenoid-9',10'-cleaving dioxygenase

organism: Mustela putorius furo

substrate_name: all-trans-beta-carotene

enzyme: carotenoid-9',10'-cleaving dioxygenase

substrate: all-trans-beta-carotene


organism: Streptomyces galilaeus

substrate_name: rhodosaminyl aklavinone (with TDP-L-daunosamine as sugar donor)

proof_lines: kcat is 2.1 sec(-1) for transferase activity with rhodosaminyl aklavinone as sugar acceptor and TDP-L-daunosamine as sugar donor. kcat is 5.4 sec(-1) for transferase activity with idarubicin as sugar acceptor and TDP-L-2-deoxyfucose as suga


enzyme_display_name: acylpyruvate hydrolase

substrate_name: enol-oxaloacetate

proof_lines: kcat is 31.1 sec(-1) with enol-oxaloacetate as substrate.

enzyme: acylpyruvate hydrolase

substrate: enol-oxaloacetate


organism: Mus musculus

substrate_name: oxaloacetate

proof_lines: kcat is 210 nmol/min/mg for the decarboxylation of oxaloacetate. kcat is 140 nmol/min/mg for the hydrolysis of acetylpyruvate.

substrate: oxaloacetate


enzyme_display_name: ethylmalonyl-CoA decarboxylase

substrate_name: (S)-ethylmalonyl-CoA (in absence of ATP)

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 10 sec(-1) with (S)-ethylmalonyl-CoA as substrate (in presence of 5 mM ATP). kcat is 1.68 sec(-1) with (S)-methylmalonyl-CoA as substrate (in presence of 5 mM ATP).

enzyme: ethylmalonyl-CoA decarboxylase


substrate_name: beta-Carotene; O2

sequence_source: UniProtKB direct accession lookup: Q7XJM2

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

substrate: beta-Carotene; O2


substrate_name: beta-carotene

sequence_source: UniProtKB direct accession lookup: Q9BYV7

substrate: beta-carotene


substrate_name: dTDP-beta-L-daunosamine

sequence_source: UniProtKB direct accession lookup: Q9L555

substrate: dTDP-beta-L-daunosamine


substrate_name: H2O; Guanosine 3'-diphosphate 5'-triphosphate

sequence_source: UniProtKB direct accession lookup: P9WHG9


substrate_name: ppGpp

sequence_source: UniProtKB direct accession lookup: Q9I686

proof_lines: presence of Mn2+, 37°C, pH not specified in the publication

substrate: ppGpp


substrate_name: Acetylpyruvate; H2O

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 direct accession lookup: Q6P587

proof_lines:
at pH 7.4 and 25°C
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=25°C, pH=7.4

source_databases_merged: sabio_rk brenda skid

substrate: Acetylpyruvate; H2O


substrate_name: (S)-Ethylmalonyl-CoA

sequence_source: UniProtKB direct accession lookup: Q9D9V3

assay_conditions_summary: pH 7.1; 303.15 K; cofactor CoA

substrate: (S)-Ethylmalonyl-CoA


substrate_name: lutein

substrate: lutein


substrate_name: rhodosaminyl aklavinone

sequence_source: UniProtKB reviewed accession Q9L555 (AKNK_STRGJ), queried by EC 2.4.1.327 and Streptomyces galilaeus

proof_lines: with TDP-L-2-deoxyfucose as cosubstrate, in 75 mM Tris (pH 7.5), 12 mM MgCl2, at 25°C

proof_lines: with TDP-L-daunosamine as cosubstrate, in 75 mM Tris (pH 7.5), 12 mM MgCl2, at 25°C

substrate: rhodosaminyl aklavinone


organism: Drosophila melanogaster

km_display: Not reported

sequence_source: UniProtKB reviewed accession Q9VAM9 (MESH1_DROME), queried by EC 3.1.7.2 and Drosophila melanogaster

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


proof_lines: pH 8.0, 30°C, kcat is reduced 2fold in the presence of the complex containing tRNA, ribosomes, and mRNA

proof_lines: pH 8.0, 30°C, KM is increased 3fold in the presence of the complex containing tRNA, ribosomes, and mRNA


substrate_name: (S)-ethylmalonyl-CoA

sequence_source: UniProtKB reviewed accession Q9D9V3 (ECHD1_MOUSE), queried by EC 4.1.1.94 and Mus musculus

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ATP

proof_lines: pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-

proof_lines: pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-

substrate: (S)-ethylmalonyl-CoA


enzyme_display_name: tyrosine N-monooxygenase

organism: Sorghum bicolor

substrate_name: L-tyrosine (in the presence of 15 mM NaCl)

proof_lines: kcat is 198 min(-1) in the presence of 15 mM NaCl. kcat is 228 min(-1) in the absence of added salt.

enzyme: tyrosine N-monooxygenase


substrate_name: L-tyrosine

sequence_source: UniProtKB reviewed accession Q43135 (C79A1_SORBI)

assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADPH

proof_lines: in reconstitution experiments using Sorghum bicolor

proof_lines: purified recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C

substrate: L-tyrosine


substrate_name: L-Tyrosine

sequence_source: UniProtKB reviewed accession Q43135 direct REST lookup

substrate: L-Tyrosine


substrate_name: NADPH; H+; L-Tyrosine; O2

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADP+

proof_lines:
pH 7.9, 25°C
presence of 0.15 mM NaCl, pH 7.9, 25°C
pH 7.9, 30°C

substrate: NADPH; H+; L-Tyrosine; O2


enzyme_display_name: geranyl diphosphate diphosphatase

organism: Ocimum basilicum

substrate_name: geranyl diphosphate

smiles: CC(=CCC/C(=C/COP(=O)(O)OP(=O)(O)O)/C)C

proof_lines: kcat is 0.8 sec(-1) with geranyl diphosphate as substrate.

enzyme: geranyl diphosphate diphosphatase

substrate: geranyl diphosphate


organism: Cinnamomum tenuipile


organism: Camptotheca acuminata

sequence_source: UniProtKB REST direct lookup for A0A109P1X1


organism: Catharanthus roseus


sequence_source: UniProtKB reviewed accession Q8GUE4 direct lookup and identity reuse cache source_record sequence


substrate_name: Geranyl diphosphate; H2O

sequence_source: Reconstructed from UniProtKB reviewed accession Q6USK1 and SABIO-RK modifier label starts with Met-44

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: SABIO-RK modifier species: geranyl diphosphate diphosphatase(Enzyme) mutant truncated starts with Met-44

substrate: Geranyl diphosphate; H2O


substrate_name: H2O; Geranyl diphosphate

sequence_source: Reconstructed from UniProtKB reviewed accession Q6USK1 and SABIO-RK modifier label starts with Ser-35

proof_lines: SABIO-RK modifier species: geranyl diphosphate diphosphatase(Enzyme) mutant truncated starts with Ser-35

substrate: H2O; Geranyl diphosphate


substrate_name: Geranyl diphosphate

sequence_source: UniProtKB reviewed accession Q6USK1 direct lookup and identity reuse cache source_record sequence

smiles: CC(C)=CCC/C(C)=C/COP(=O)(O)OP(=O)(O)O

substrate: Geranyl diphosphate


substrate_name: Acetylpyruvate

sequence_source: UniProtKB reviewed accession Q6P587 direct lookup plus Expasy EC 3.7.1.5 cross-reference

proof_lines: pH 7.4, 22°C, recombinant wild-type FAHD1

substrate: Acetylpyruvate


sequence_source: Canonical accession context from UniProtKB Q6P587; row-specific H30A variant sequence unresolved

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


sequence_source: Canonical accession context from UniProtKB Q6P587; row-specific E33A variant sequence unresolved


substrate_name: oxaloacetate

substrate: oxaloacetate


sequence_source: UniProtKB reviewed accession Q8R0F8 direct lookup plus Expasy EC 3.7.1.5 cross-reference


enzyme_display_name: 2-oxoglutarate decarboxylase

organism: Mycobacterium smegmatis

sequence_source: UniProtKB reviewed accession A0R2B1

enzyme: 2-oxoglutarate decarboxylase


smiles: O=C(O)CCC(=O)C(=O)O


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WIS5


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: allantoate deiminase

organism: Oryza sativa subsp. japonica

substrate_name: allantoate

enzyme: allantoate deiminase

substrate: allantoate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


mutation_signature: Met44-truncated mutant

sequence_source: UniProtKB:Q6USK1 plus PMID:14657409 PMC full-text Met-44 truncation mapping


mutation_signature: Ser35 truncated mutant

sequence_source: UniProtKB:Q6USK1 plus PMID:14657409 PMC full-text Ser-35 truncation mapping


sequence_source: UniProtKB:Q6USK1 reviewed entry linked to PMID:14657409


organism: Agrobacterium sp.


enzyme_display_name: pseudouridine kinase

organism: Arabidopsis thaliana

substrate_name: pseudouridine

enzyme: pseudouridine kinase

substrate: pseudouridine


organism: Escherichia coli

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Glycine max

substrate_name: Allantoate

substrate: Allantoate


organism: Metabacillus fastidiosus


organism: Phaseolus vulgaris


organism: Euglena gracilis


organism: Oenococcus oeni


organism: Picosynechococcus sp. PCC 7002

proof_lines:
pH 7.0, 25°C
at pH 7.0 and 25°C


organism: Homo sapiens

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB Q15047 REST lookup 2026-06-16

substrate: S-adenosyl-L-methionine


organism: Pseudomonas putida

substrate_name: N-acetyl-D-muramate 6-phosphate

sequence_source: UniProtKB Q88M11 REST lookup 2026-06-16

proof_lines:
pH 7.6, 22°C
at pH 7.6 and 22°C

substrate: N-acetyl-D-muramate 6-phosphate


sequence_source: UniProtKB I1L153 REST lookup 2026-06-16


sequence_source: UniProtKB C0M0V4 REST lookup 2026-06-16


organism: Oryza sativa

sequence_source: UniProtKB Q655X8 REST lookup 2026-06-16


sequence_source: UniProtKB A6YS26 REST lookup 2026-06-16


proof_lines: kcat is 0.23 sec(-1) with pseudouridine as substrate (PubMed:31907295). kcat is 5.28 sec(-1) with pseudouridine as substrate (PubMed:33290549). kcat is 5.80 sec(-1) with ATP as substrate (PubMed:33290549).


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: N-acetylmuramate 6-phosphate (at pH 7.6 and 22 degrees Celsius)

proof_lines: kcat is 0.88 sec(-1) (at pH 7.6 and 22 degrees Celsius).


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: rubredoxin--NAD(+) reductase

organism: Clostridium acetobutylicum

substrate_name: NADH

sequence_source: UniProtKB reviewed canonical sequence Q9AL95 retrieved 2026-06-16

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

enzyme: rubredoxin--NAD(+) reductase

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: ATP; Pseudouridine

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

sequence_source: UniProtKB reviewed canonical sequence P30235 retrieved 2026-06-16

substrate: ATP; Pseudouridine


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

substrate_name: rubredoxin

assay_conditions_summary: cofactor NADPH

substrate: rubredoxin


organism: Escherichia coli (strain K12)

substrate_name: pseudouridine (in the presence of 0.5 mM ATP)


organism: Bos taurus

sequence_source: UniProtKB reviewed accession Q2TBQ8 REST/FASTA lookup on 2026-06-16


organism: Mus musculus

substrate_name: D-glucose (at pH 7.1 in the presence of NADP)


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: glucose-6-phosphate (at 25 degrees Celsius)


organism: Methanothermobacter thermautotrophicus

substrate_name: sn-glycerol 1-phosphate

substrate: sn-glycerol 1-phosphate


organism: Thermoplasma acidophilum

substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: small monomeric GTPase

substrate_name: GTP

proof_lines: quite low, increased GTP hydrolysis by action of guanine nucleotide release proteins, promoting replacement of bound GDP by GTP

enzyme: small monomeric GTPase

substrate: GTP


enzyme_display_name: maleate hydratase

organism: Arthrobacter sp.

substrate_name: Maleate

enzyme: maleate hydratase

substrate: Maleate


organism: Ectopseudomonas oleovorans

substrate_name: citraconate

substrate: citraconate


enzyme_display_name: carbonyl sulfide hydrolase

organism: Thiobacillus thioparus

substrate_name: carbonyl sulfide

enzyme: carbonyl sulfide hydrolase

substrate: carbonyl sulfide


proof_lines: kcat is 5.4 sec(-1) with GTP as substrate.


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

substrate_name: G1P (at 55 degrees Celsius and pH 8)

substrate: G1P (at 55 degrees Celsius and pH 8)


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: G-1,3-P (at 55 degrees Celsius and pH 7)


organism: Homo sapiens


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


enzyme_display_name: loganate O-methyltransferase

organism: Catharanthus roseus

substrate_name: loganic acid (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 0.31 sec(-1) with loganic acid as substrate (at pH 7.5 and 30 degrees Celsius).

enzyme: loganate O-methyltransferase


substrate_name: 23S rRNA within 50S ribosomal subunits

substrate: 23S rRNA within 50S ribosomal subunits


enzyme_display_name: 3-isopropylmalate dehydratase

enzyme: 3-isopropylmalate dehydratase


substrate_name: loganic acid

substrate: loganic acid


organism: Ophiorrhiza pumila

substrate_name: loganate

proof_lines: pH and temperature not specified in the publication

substrate: loganate


organism: Acidithiobacillus thiooxidans


organism: Candida maltosa

substrate_name: beta-carboxy-beta-hydroxyisocaproate

substrate: beta-carboxy-beta-hydroxyisocaproate


organism: Neurospora crassa

substrate_name: dimethylcitraconate

substrate: dimethylcitraconate


organism: Saccharomyces cerevisiae

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


organism: Escherichia coli

substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0C0R7 direct REST/FASTA check on 2026-06-16 plus D83A substitution from selected source mutation_signature and applied mutation signature D83A to reconstruct the assayed variant sequence.

substrate: S-Adenosyl-L-methionine


sequence_source: UniProtKB:P0C0R7 direct REST/FASTA check on 2026-06-16


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


sequence_source: UniProtKB:Q15047 direct REST/FASTA check on 2026-06-16

proof_lines: substrate [histone H3 peptide 1-15]-N6,N6-dimethyl-L-lysine9, pH 7.6, 23°C

proof_lines: substrate [histone H3 peptide 1-15]-N6,N6-dimethyl-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C


sequence_source: UniProtKB:B2KPR3 direct REST/FASTA check on 2026-06-16

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


organism: Methanothermobacter marburgensis

substrate_name: Geranylgeranyl diphosphate

sequence_source: UniProtKB:P0C882 direct REST/FASTA check on 2026-06-16

substrate: Geranylgeranyl diphosphate


substrate_name: sn-Glyceryl phosphate

smiles: O=P(O)(O)OCC(O)CO

substrate: sn-Glyceryl phosphate


sequence_source: UniProtKB:Q9HJH3 direct REST/FASTA check on 2026-06-16


sequence_source: UniProtKB:H1AAP2 direct REST/FASTA check on 2026-06-16

smiles: O=C=S


proof_lines:
at pH 8.5 and 30°C
Raw SKiD Env: Temp=30°C, pH=8.5


organism: Streptococcus pneumoniae

sequence_source: UniProtKB:P0A3C4 direct REST/FASTA check on 2026-06-16


organism: Methanocaldococcus jannaschii


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


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


organism: Acinetobacter calcoaceticus

substrate_name: NADH

proof_lines: reaction with 2,6-dichloroindophenol or Fe(CN)63-

substrate: NADH


organism: Streptomyces venezuelae

proof_lines: kcat is 92 min(-1) with dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose as substrate. kcat is 4.2 min(-1) with dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose as substrate.


organism: Bos taurus

proof_lines: synthetic 6-phosphogluconolactone, pH 6.5

proof_lines: synthetic 6-phosphogluconolactone, pH 7.4


organism: Dicentrarchus labrax


organism: Rattus norvegicus


organism: Alcanivorax borkumensis

sequence_source: UniProtKB REST lookup accession Q0VTB0 on 2026-06-16

assay_conditions_summary: pH 8; 318.15 K; cofactor NADH


sequence_source: UniProtKB REST lookup accession Q9ZGH6 on 2026-06-16


proof_lines: pH 7.5, 24°C, cosubstrate: 3.0 mM S-adenosyl-L-methionine


substrate_name: H2O; 6-Phospho-D-glucono-1,5-lactone

sequence_source: UniProtKB REST lookup accession Q2TBQ8 on 2026-06-16

substrate: H2O; 6-Phospho-D-glucono-1,5-lactone


organism: Giardia duodenalis


enzyme_display_name: L-threo-3-deoxy-hexylosonate aldolase

organism: Trichoderma reesei

enzyme: L-threo-3-deoxy-hexylosonate aldolase


enzyme_display_name: deaminated glutathione amidase

organism: Arabidopsis thaliana

proof_lines: kcat is 4.2 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine as substrate (PubMed:30692244). kcat is 3.0 sec(-1) with ophthalmate as substrate (PubMed:30692244).

enzyme: deaminated glutathione amidase


organism: Mus musculus

substrate_name: N-(4-oxoglutarate)-L-cysteinylglycine (at pH 8.5)

proof_lines: kcat is 1.6 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine as substrate.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 3.6 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine as substrate.

substrate: N-(4-oxoglutarate)-L-cysteinylglycine (at pH 8.5)


enzyme_display_name: thermospermine synthase

organism: Thermus thermophilus

substrate_name: S-Adenosylmethioninamine

sequence_source: UniProtKB:Q5SK28 direct lookup, release 2026_02, checked 2026-06-16

enzyme: thermospermine synthase

substrate: S-Adenosylmethioninamine


sequence_source: UniProtKB:P27833 direct lookup, release 2026_02, checked 2026-06-16


proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5


enzyme_display_name: sedoheptulokinase

substrate_name: Sedoheptulose

sequence_source: UniProtKB:Q9D5J6 direct lookup, release 2026_02, checked 2026-06-16

enzyme: sedoheptulokinase

substrate: Sedoheptulose


substrate_name: sedoheptulose

substrate: sedoheptulose


enzyme_display_name: CTP-dependent riboflavin kinase

organism: Metallosphaera yellowstonensis

substrate_name: riboflavin

sequence_source: UniProtKB:H2C8H2 direct lookup, release 2026_02, checked 2026-06-16

enzyme: CTP-dependent riboflavin kinase

substrate: riboflavin


substrate_name: CTP

sequence_source: UniProtKB:Q60365 direct lookup, release 2026_02, checked 2026-06-16

proof_lines:
pH 7.2, 70°C
Raw SKiD Env: Temp=70°C, pH=7.2

substrate: CTP


organism: Pyrobaculum sp. WP30


enzyme_display_name: anhydro-N-acetylmuramic acid kinase

organism: Escherichia coli

sequence_source: UniProtKB:P77570 direct lookup, release 2026_02, checked 2026-06-16

enzyme: anhydro-N-acetylmuramic acid kinase


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I5Q5 direct lookup, release 2026_02, checked 2026-06-16

proof_lines: in 50 mM HEPES, pH 7.5, 10 mM MgCl2, and 50 mM KCl, at 37°C


enzyme_display_name: glycoprotein-mannosyl O(6)-kinase

substrate_name: ATP

sequence_source: UniProtKB:Q3TUA9 direct lookup, release 2026_02, checked 2026-06-16

proof_lines: pH and temperature not specified in the publication, recombinant murine POMK catalytic domain

enzyme: glycoprotein-mannosyl O(6)-kinase

substrate: ATP


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

sequence_source: UniProtKB:P16687 direct lookup, release 2026_02, checked 2026-06-16

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


substrate_name: GTP

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

substrate: GTP


enzyme_display_name: tRNA uracil 4-sulfurtransferase

sequence_source: UniProtKB:P77718 direct lookup, release 2026_02, checked 2026-06-16

enzyme: tRNA uracil 4-sulfurtransferase


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


enzyme_display_name: L-asparagine oxygenase

organism: Streptomyces coelicolor

substrate_name: L-asparagine

enzyme: L-asparagine oxygenase

substrate: L-asparagine


organism: Zea mays

substrate_name: DIBOA glucoside

substrate: DIBOA glucoside


enzyme_display_name: phenylalanine N-monooxygenase

substrate_name: L-phenylalanine

enzyme: phenylalanine N-monooxygenase

substrate: L-phenylalanine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


enzyme_display_name: geraniol 8-hydroxylase

organism: Catharanthus roseus

substrate_name: geraniol

smiles: CC(C)=CCC/C(C)=C/CO

enzyme: geraniol 8-hydroxylase

substrate: geraniol


proof_lines:
pH 7.4, 27°C
pH 8.0, 30°C, recombinant enzyme


enzyme_display_name: 4-aminobenzoate N-oxygenase

organism: Streptomyces thioluteus

proof_lines:
pH 7.4, 20°C
Raw SKiD Env: Temp=20°C, pH=7.4

enzyme: 4-aminobenzoate N-oxygenase


enzyme_display_name: L-methionine (S)-S-oxide reductase

substrate_name: L-Methionine S-oxide

enzyme: L-methionine (S)-S-oxide reductase

substrate: L-Methionine S-oxide


enzyme_display_name: mitomycin 6-O-methyltransferase

organism: Streptomyces lavendulae

substrate_name: 7-demethylmitomycin A

enzyme: mitomycin 6-O-methyltransferase

substrate: 7-demethylmitomycin A


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

organism: Agrobacterium tumefaciens

substrate_name: pyruvate

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

substrate: pyruvate


organism: Botryococcus braunii

substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Deinococcus radiodurans

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H304A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'D-glyceraldehyde 3-phosphate', enzyme-form row 'H304A': column 'KM (mM)' = 0.08; column 'kcat/KM (s-1 M-1)' = 1.1 x 10^4; column 'kcat (s-1)' = 0.90. captured primary segment: Table 2 | substrate D-glyceraldehyde 3-phosphate | Deinococcus radiodurans DXS H304A | KM 0.08 mM | kcat 0.90 s-1 | kcat/KM 1.1 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.08 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.08 mM. kcat: printed Table 2 cell 0.90 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.9 s^(-1). kcat/KM: printed Table 2 cell 1.1 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 11000 / 1000 = 11.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.9 / 0.08 = 11.25 s-1 mM-1, against the printed catalytic-efficiency cell 1.1 x 10^4 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'D-glyceraldehyde 3-phosphate', printed enzyme-form row 'H304A': kcat = 0.90 s-1; KM = 0.08 mM; printed kcat/KM = 1.1 x 10^4 s-1 M-1.

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature D430A to reconstruct the assayed variant sequence.

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

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'D430A': column 'KM (mM)' = 0.52; column 'kcat/KM (s-1 M-1)' = 1.4 x 10^4; column 'kcat (s-1)' = 7.2. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS D430A | KM 0.52 mM | kcat 7.2 s-1 | kcat/KM 1.4 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.52 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.52 mM. kcat: printed Table 2 cell 7.2 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 7.2 s^(-1). kcat/KM: printed Table 2 cell 1.4 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 14000 / 1000 = 14.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.2 / 0.52 = 13.846153846153847 s-1 mM-1, against the printed catalytic-efficiency cell 1.4 x 10^4 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'D430A': kcat = 7.2 s-1; KM = 0.52 mM; printed kcat/KM = 1.4 x 10^4 s-1 M-1.


organism: Methanococcus maripaludis

substrate_name: Sulfide

substrate: Sulfide


enzyme_display_name: keratan sulfotransferase

organism: Homo sapiens

substrate_name: 3'-Phosphoadenylyl sulfate

enzyme: keratan sulfotransferase

substrate: 3'-Phosphoadenylyl sulfate


enzyme_display_name: (3S)-malyl-CoA thioesterase

organism: Cereibacter sphaeroides

substrate_name: (S)-malyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 1, Mcl2 thioester cleavage: kcat 110 s^-1; target-substrate Km 0.09 mM; printed kcat/Km 1.2 × 10^6 M^-1 s^-1 = 1200 s^-1 mM^-1. Current 1222.2222222222222 lies in the printed-efficiency rounding interval [1150, 1250) s^-1 mM^-1.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=110 s^-1 and target-substrate Km=0.09 mM. Their stored-precision quotient is 110 / 0.09 = 1222.2222222222222 s^-1 mM^-1. Printed efficiency normalizes separately to 1200 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=110 raw_unit=s^-1; Km raw_value=0.09 raw_unit=mM; printed kcat/Km raw_value=1.2 × 10^6 raw_unit=M^-1 s^-1

row_label: Mcl2 / thioester cleavage

table_label: Table 1: Molecular and catalytic properties of recombinant (3S)-malyl-CoA/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase from R. sphaeroides

enzyme: (3S)-malyl-CoA thioesterase

substrate: (S)-malyl-CoA


proof_lines: pH 7.5, 30°C, in the presence of divalent cations (Mg2+ or Mn2+)


organism: Rhodobacter sphaeroides

substrate_name: L-Malyl-CoA

substrate: L-Malyl-CoA


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Arabidopsis thaliana

substrate_name: S-D-lactoylglutathione

enzyme: hydroxyacylglutathione hydrolase

substrate: S-D-lactoylglutathione


substrate_name: (R)-S-Lactoylglutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession_mutation_reconstruction and applied mutation signature D58C to reconstruct the assayed variant sequence.

substrate: (R)-S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession_mutation_reconstruction and applied mutation signature H54N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H82A to reconstruct the assayed variant sequence.

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'H82A': column 'KM (mM)' = 0.23; column 'kcat/KM (s-1 M-1)' = 1.7 x 10^3; column 'kcat (s-1)' = 0.38. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS H82A | KM 0.23 mM | kcat 0.38 s-1 | kcat/KM 1.7 x 10^3 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.23 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.23 mM. kcat: printed Table 2 cell 0.38 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.38 s^(-1). kcat/KM: printed Table 2 cell 1.7 x 10^3 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 1700 / 1000 = 1.7 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.38 / 0.23 = 1.6521739130434783 s-1 mM-1, against the printed catalytic-efficiency cell 1.7 x 10^3 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'H82A': kcat = 0.38 s-1; KM = 0.23 mM; printed kcat/KM = 1.7 x 10^3 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature H434A to reconstruct the assayed variant sequence.


column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'D-glyceraldehyde 3-phosphate', enzyme-form row 'H82A': column 'KM (mM)' = 0.03; column 'kcat/KM (s-1 M-1)' = 1.3 x 10^4; column 'kcat (s-1)' = 0.37. captured primary segment: Table 2 | substrate D-glyceraldehyde 3-phosphate | Deinococcus radiodurans DXS H82A | KM 0.03 mM | kcat 0.37 s-1 | kcat/KM 1.3 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.03 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.03 mM. kcat: printed Table 2 cell 0.37 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.37 s^(-1). kcat/KM: printed Table 2 cell 1.3 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 13000 / 1000 = 13.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 0.37 / 0.03 = 12.333333333333334 s-1 mM-1, which falls outside the rounding interval of the printed cell 1.3 x 10^4 at the place value that printed literal carries, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'D-glyceraldehyde 3-phosphate', printed enzyme-form row 'H82A': kcat = 0.37 s-1; KM = 0.03 mM; printed kcat/KM = 1.3 x 10^4 s-1 M-1.


column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'H304A': column 'KM (mM)' = 1.7; column 'kcat/KM (s-1 M-1)' = 5.8 x 10^2; column 'kcat (s-1)' = 0.90. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS H304A | KM 1.7 mM | kcat 0.90 s-1 | kcat/KM 5.8 x 10^2 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 1.7 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 1.7 mM. kcat: printed Table 2 cell 0.90 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.9 s^(-1). kcat/KM: printed Table 2 cell 5.8 x 10^2 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 580 / 1000 = 0.58 s^(-1)*mM^(-1). The quotient of the two printed component cells is 0.9 / 1.7 = 0.5294117647058824 s-1 mM-1, which falls outside the rounding interval of the printed cell 5.8 x 10^2 at the place value that printed literal carries, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'H304A': kcat = 0.90 s-1; KM = 1.7 mM; printed kcat/KM = 5.8 x 10^2 s-1 M-1.


sequence_source: UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from 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: apparent value, wild type enzyme, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H434A to reconstruct the assayed variant sequence.

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'H434A': column 'KM (mM)' = 1.7; column 'kcat/KM (s-1 M-1)' = 5.9 x 10^3; column 'kcat (s-1)' = 9.9. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS H434A | KM 1.7 mM | kcat 9.9 s-1 | kcat/KM 5.9 x 10^3 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 1.7 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 1.7 mM. kcat: printed Table 2 cell 9.9 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 9.9 s^(-1). kcat/KM: printed Table 2 cell 5.9 x 10^3 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 5900 / 1000 = 5.9 s^(-1)*mM^(-1). The quotient of the two printed component cells is 9.9 / 1.7 = 5.8235294117647065 s-1 mM-1, which falls outside the rounding interval of the printed cell 5.9 x 10^3 at the place value that printed literal carries, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'H434A': kcat = 9.9 s-1; KM = 1.7 mM; printed kcat/KM = 5.9 x 10^3 s-1 M-1.


column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'wild-type': column 'KM (mM)' = 0.28; column 'kcat/KM (s-1 M-1)' = 2.6 x 10^4; column 'kcat (s-1)' = 7.4. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS wild-type | KM 0.28 mM | kcat 7.4 s-1 | kcat/KM 2.6 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.28 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.28 mM. kcat: printed Table 2 cell 7.4 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 7.4 s^(-1). kcat/KM: printed Table 2 cell 2.6 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 26000 / 1000 = 26.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.4 / 0.28 = 26.428571428571427 s-1 mM-1, against the printed catalytic-efficiency cell 2.6 x 10^4 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'wild-type': kcat = 7.4 s-1; KM = 0.28 mM; printed kcat/KM = 2.6 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature D430A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature N181A to reconstruct the assayed variant sequence.

column_label: Table 1: Domain I mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 23), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'N181A': column 'KM,app (mM)' = 0.03 ± 0.01; column 'kcat,app (s-1)' = 0.43 ± 0.02; column '(kcat/KM)app (s-1 M-1)' = 1.4 x 10^4; unheaded relative-efficiency column = 0.09.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.43 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.43 s^(-1); the exported value is 0.43 s^(-1). Km: printed Table 1 cell 0.03 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.03 mM; the exported value is 0.03 mM. kcat/KM: printed Table 1 cell 1.4 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^4 / 1000 = 14.0 s^-1 mM^-1; the paper value is 14.0 s^(-1)*mM^(-1); the exported value is 14.333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Protein row 'N181A', GAP as the variable substrate: KM,app = 0.03 mM; kcat,app = 0.43 s-1; printed (kcat/KM)app = 1.4 x 10^4 s-1 M-1.

row_label: Table 1, Protein row 'N181A', with GAP as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature Y395A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme Y395A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature R423A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme R423A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature N181A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme N181A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H434K to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H434K': column 'KM,app (mM)' = 1.7 ± 0.1; column 'kcat,app (s-1)' = 9.9 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 5.9 x 10^3; unheaded relative-efficiency column = 0.2+.

normalized_value_unit_evidence: kcat: printed Table 4 cell 9.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 9.9 s^(-1); the exported value is 9.9 s^(-1). Km: printed Table 4 cell 1.7 mM; the printed unit is already mM, no unit conversion applies; the paper value is 1.7 mM; the exported value is 0.05 mM. kcat/KM: printed Table 4 cell 5.9 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^3 / 1000 = 5.9 s^-1 mM^-1; the paper value is 5.9 s^(-1)*mM^(-1); the exported value is 198.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Protein row 'H434K', pyruvate as the variable substrate: KM,app = 1.7 mM; kcat,app = 9.9 s-1; printed (kcat/KM)app = 5.9 x 10^3 s-1 M-1.

row_label: Table 4, Protein row 'H434K', with pyruvate as the variable substrate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature Y395A to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395A': column 'KM,app (mM)' = 0.16 ± 0.01; column 'kcat,app (s-1)' = 3.6 ± 0.1; column '(kcat/KM)app (s-1 M-1)' = 2.2 x 10^4; unheaded relative-efficiency column = 0.8.

normalized_value_unit_evidence: kcat: printed Table 4 cell 3.6 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.6 s^(-1); the exported value is 3.6 s^(-1). Km: printed Table 4 cell 0.16 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.16 mM; the exported value is 0.16 mM. kcat/KM: printed Table 4 cell 2.2 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^4 / 1000 = 22.0 s^-1 mM^-1; the paper value is 22.0 s^(-1)*mM^(-1); the exported value is 22.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Protein row 'Y395A', pyruvate as the variable substrate: KM,app = 0.16 mM; kcat,app = 3.6 s-1; printed (kcat/KM)app = 2.2 x 10^4 s-1 M-1.

row_label: Table 4, Protein row 'Y395A', with pyruvate as the variable substrate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature R423A to reconstruct the assayed variant sequence.

column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'R423A': column 'KM,app (mM)' = 12 ± 3.2; column 'kcat,app (s-1)' = 1.7 ± 0.3; column '(kcat/KM)app (s-1 M-1)' = 1.4 x 10^2; unheaded relative-efficiency column = 9 x 10^-4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.7 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.7 s^(-1); the exported value is 1.7 s^(-1). Km: printed Table 3 cell 12 mM; the printed unit is already mM, no unit conversion applies; the paper value is 12.0 mM; the exported value is 12.0 mM. kcat/KM: printed Table 3 cell 1.4 x 10^2 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^2 / 1000 = 0.14 s^-1 mM^-1; the paper value is 0.14 s^(-1)*mM^(-1); the exported value is 0.14166666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'R423A', GAP as the variable substrate: KM,app = 12 mM; kcat,app = 1.7 s-1; printed (kcat/KM)app = 1.4 x 10^2 s-1 M-1.

row_label: Table 3, Protein row 'R423A', with GAP as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature H304A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme H304A, at pH 8.0 and 37°C


substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB reviewed accession Q9RUB5 REST lookup on 2026-06-16

proof_lines: inhibition with respect to pyruvate, at pH 8.0 and 37°C

proof_lines: inhibition with respect to D-glyceraldehyde 3-phosphate, at pH 8.0 and 37°C

substrate: Unknown


column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H434A': column 'KM,app (mM)' = 0.23 ± 0.01; column 'kcat,app (s-1)' = 9.6 ± 0.3; column '(kcat/KM)app (s-1 M-1)' = 4.2 x 10^4; unheaded relative-efficiency column = 0.3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.6 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 9.6 s^(-1); the exported value is 9.9 s^(-1). Km: printed Table 3 cell 0.23 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.23 mM; the exported value is 0.23 mM. kcat/KM: printed Table 3 cell 4.2 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^4 / 1000 = 42.0 s^-1 mM^-1; the paper value is 42.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 3, Protein row 'H434A', GAP as the variable substrate: KM,app = 0.23 mM; kcat,app = 9.6 s-1; printed (kcat/KM)app = 4.2 x 10^4 s-1 M-1.

row_label: Table 3, Protein row 'H434A', with GAP as the variable substrate


column_label: Table 2: Domain I mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 24), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H82A': column 'KM,app (mM)' = 0.23 ± 0.02; column 'kcat,app (s-1)' = 0.38 ± 0.01; column '(kcat/KM)app (s-1 M-1)' = 1.7 x 10^3; unheaded relative-efficiency column = 0.07.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.38 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.38 s^(-1); the exported value is 0.38 s^(-1). Km: printed Table 2 cell 0.23 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.23 mM; the exported value is 0.03 mM. kcat/KM: printed Table 2 cell 1.7 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^3 / 1000 = 1.7 s^-1 mM^-1; the paper value is 1.7 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 2, Protein row 'H82A', pyruvate as the variable substrate: KM,app = 0.23 mM; kcat,app = 0.38 s-1; printed (kcat/KM)app = 1.7 x 10^3 s-1 M-1.

row_label: Table 2, Protein row 'H82A', with pyruvate as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RUB5 REST lookup plus selected-row mutation_signature D430A and applied mutation signature D430A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme D430A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature Y395F to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395F': column 'KM,app (mM)' = 0.19 ± 0.01; column 'kcat,app (s-1)' = 2.9 ± 0.02; column '(kcat/KM)app (s-1 M-1)' = 1.6 x 10^4; unheaded relative-efficiency column = 0.6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 2.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 2.9 s^(-1); the exported value is 5.9 s^(-1). Km: printed Table 4 cell 0.19 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.19 mM; the exported value is 0.19 mM. kcat/KM: printed Table 4 cell 1.6 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^-1 mM^-1; the paper value is 16.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 4, Protein row 'Y395F', pyruvate as the variable substrate: KM,app = 0.19 mM; kcat,app = 2.9 s-1; printed (kcat/KM)app = 1.6 x 10^4 s-1 M-1.

row_label: Table 4, Protein row 'Y395F', with pyruvate as the variable substrate


column_label: Table 2: Domain I mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 24), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'N181A': column 'KM,app (mM)' = 0.17 ± 0.02; column 'kcat,app (s-1)' = 3.3 ± 0.1; column '(kcat/KM)app (s-1 M-1)' = 1.9 x 10^4; unheaded relative-efficiency column = 0.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.3 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.3 s^(-1); the exported value is 3.3 s^(-1). Km: printed Table 2 cell 0.17 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.17 mM; the exported value is 0.17 mM. kcat/KM: printed Table 2 cell 1.9 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^4 / 1000 = 19.0 s^-1 mM^-1; the paper value is 19.0 s^(-1)*mM^(-1); the exported value is 19.41176470588235 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Protein row 'N181A', pyruvate as the variable substrate: KM,app = 0.17 mM; kcat,app = 3.3 s-1; printed (kcat/KM)app = 1.9 x 10^4 s-1 M-1.

row_label: Table 2, Protein row 'N181A', with pyruvate as the variable substrate


normalized_value_unit_evidence: kcat: printed Table 4 cell 2.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 2.9 s^(-1); the exported value is 2.9 s^(-1). Km: printed Table 4 cell 0.19 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.19 mM; the exported value is 0.19 mM. kcat/KM: printed Table 4 cell 1.6 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^-1 mM^-1; the paper value is 16.0 s^(-1)*mM^(-1); the exported value is 15.26315789473684 s^(-1)*mM^(-1).

table_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26)


column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395A': column 'KM,app (mM)' = 0.67 ± 0.05; column 'kcat,app (s-1)' = 3.9 ± 0.1; column '(kcat/KM)app (s-1 M-1)' = 5.8 x 10^3; unheaded relative-efficiency column = 0.04.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.9 s^(-1); the exported value is 3.9 s^(-1). Km: printed Table 3 cell 0.67 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.67 mM; the exported value is 0.59 mM. kcat/KM: printed Table 3 cell 5.8 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 5.8 x 10^3 / 1000 = 5.8 s^-1 mM^-1; the paper value is 5.8 s^(-1)*mM^(-1); the exported value is 6.610169491525424 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'Y395A', GAP as the variable substrate: KM,app = 0.67 mM; kcat,app = 3.9 s-1; printed (kcat/KM)app = 5.8 x 10^3 s-1 M-1.

row_label: Table 3, Protein row 'Y395A', with GAP as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RUB5 REST lookup plus selected-row mutation_signature R423K and applied mutation signature R423K to reconstruct the assayed variant sequence.


normalized_value_unit_evidence: kcat: printed Table 4 cell 9.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 9.9 s^(-1); the exported value is 9.9 s^(-1). Km: printed Table 4 cell 1.7 mM; the printed unit is already mM, no unit conversion applies; the paper value is 1.7 mM; the exported value is 0.05 mM. kcat/KM: printed Table 4 cell 5.9 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^3 / 1000 = 5.9 s^-1 mM^-1; the paper value is 5.9 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature R423K to reconstruct the assayed variant sequence.

column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'R423K': column 'KM,app (mM)' = 0.60 ± 0.1; column 'kcat,app (s-1)' = 6.4 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 1.1 x 10^4; unheaded relative-efficiency column = 0.07.

normalized_value_unit_evidence: kcat: printed Table 3 cell 6.4 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 6.4 s^(-1); the exported value is 6.4 s^(-1). Km: printed Table 3 cell 0.60 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.6 mM; the exported value is 0.6 mM. kcat/KM: printed Table 3 cell 1.1 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^-1 mM^-1; the paper value is 11.0 s^(-1)*mM^(-1); the exported value is 10.666666666666668 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'R423K', GAP as the variable substrate: KM,app = 0.60 mM; kcat,app = 6.4 s-1; printed (kcat/KM)app = 1.1 x 10^4 s-1 M-1.

row_label: Table 3, Protein row 'R423K', with GAP as the variable substrate


column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395F': column 'KM,app (mM)' = 0.59 ± 0.04; column 'kcat,app (s-1)' = 5.9 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 1.0 x 10^4; unheaded relative-efficiency column = 0.07.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 5.9 s^(-1); the exported value is 5.9 s^(-1). Km: printed Table 3 cell 0.59 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.59 mM; the exported value is 7.7 mM. kcat/KM: printed Table 3 cell 1.0 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.0 x 10^4 / 1000 = 10.0 s^-1 mM^-1; the paper value is 10.0 s^(-1)*mM^(-1); the exported value is 0.7662337662337663 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'Y395F', GAP as the variable substrate: KM,app = 0.59 mM; kcat,app = 5.9 s-1; printed (kcat/KM)app = 1.0 x 10^4 s-1 M-1.

row_label: Table 3, Protein row 'Y395F', with GAP as the variable substrate


normalized_value_unit_evidence: kcat: printed Table 3 cell 6.4 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 6.4 s^(-1); the exported value is 6.4 s^(-1). Km: printed Table 3 cell 0.60 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.6 mM; the exported value is 0.06 mM. kcat/KM: printed Table 3 cell 1.1 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^-1 mM^-1; the paper value is 11.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

table_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25)


substrate_name: D-Glyceraldehyde 3-phosphate

sequence_source: UniProtKB reviewed accession P77488 REST lookup on 2026-06-16

substrate: D-Glyceraldehyde 3-phosphate


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction H54N. and applied mutation signature H54N to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical accession O24496; 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.


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction W57N. and applied mutation signature W57N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction L9A. and applied mutation signature L9A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical accession O24496.

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

proof_lines: recombinant wild-type enzyme, pH 7.2, 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction W57D. and applied mutation signature W57D to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical accession O24496; double-variant sequence not accepted.

proof_lines: recombinant mutants W57N and K65A, pH 7.2, 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction K65A. and applied mutation signature K65A to reconstruct the assayed variant sequence.


proof_lines: recombinant enzyme grown in medium not supplemented with metal ions, pH 7.2, 25°C

proof_lines: recombinant enzyme grown in medium supplemented with Mn2+, pH 7.2, 25°C

proof_lines: recombinant enzyme grown in medium supplemented with Fe2+, pH 7.2, 25°C


substrate_name: S-Lactoylglutathione

source_db: brenda,skid

sequence_source: UniProt REST canonical accession Q9SID3.

proof_lines:
25°C, pH 7.2
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.2

substrate: S-Lactoylglutathione

source: brenda,skid


substrate_name: (R)-S-Mandeloylglutathione

substrate: (R)-S-Mandeloylglutathione


organism: Brassica juncea

sequence_source: UniProt REST canonical accession Q84XQ5.


sequence_source: UniProt REST canonical accession P0AC84.


sequence_source: UniProt REST canonical accession Q16775; variant sequence not accepted.


sequence_source: UniProt REST canonical accession Q16775.


organism: Salvia splendens

substrate_name: malonyl-CoA; 4'''-demalonylsalvianin

sequence_source: UniProtKB:Q6TXD2 direct lookup

assay_conditions_summary: pH 8.5; cofactor CoA

proof_lines: pH 8.5, temperature not specified in the publication

substrate: malonyl-CoA; 4'''-demalonylsalvianin


substrate_name: Malonyl-CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

substrate: Malonyl-CoA


enzyme_display_name: Kdo2-lipid IVA acyltransferase

organism: Escherichia coli

sequence_source: UniProtKB:P0ACV0 direct lookup

enzyme: Kdo2-lipid IVA acyltransferase


organism: Mycobacterium tuberculosis

substrate_name: Trehalose 2-sulfate

sequence_source: UniProtKB:P9WIK7 direct lookup

substrate: Trehalose 2-sulfate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


substrate_name: Phenylthioacetohydroximate

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

substrate: Phenylthioacetohydroximate


organism: Lachnoclostridium phytofermentans

substrate_name: L-Rhamnose

sequence_source: UniProtKB:A9KM56 direct lookup

substrate: L-Rhamnose


substrate_name: beta-D-Glucose 1-phosphate

substrate: beta-D-Glucose 1-phosphate


substrate_name: L-rhamnose; beta-D-glucose 1-phosphate

proof_lines: pH 6.5, 30°C, reverse phosphorolysis reaction, cosubstrate beta-D-glucose 1-phosphate

substrate: L-rhamnose; beta-D-glucose 1-phosphate


enzyme_display_name: sym-norspermidine synthase

organism: Pyrococcus furiosus

sequence_source: UniProtKB:Q8U4G1 direct lookup

smiles: NCCCN

enzyme: sym-norspermidine synthase


enzyme_display_name: cysteate synthase

organism: Methanosarcina acetivorans

substrate_name: sulfite

sequence_source: UniProtKB:Q8TKU7 direct lookup

enzyme: cysteate synthase

substrate: sulfite


substrate_name: L-phosphoserine

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

substrate: L-phosphoserine


enzyme_display_name: thermospermine synthase

organism: Thermus thermophilus

substrate_name: Spermidine

sequence_source: UniProtKB:Q5SK28 direct lookup

smiles: NCCCCNCCCN

enzyme: thermospermine synthase

substrate: Spermidine


substrate_name: Mitsubishine

substrate: Mitsubishine


organism: Rattus norvegicus

sequence_source: UniProt REST direct lookup 2026-06-16, accession O35952


organism: Saccharomyces cerevisiae

substrate_name: S-D-mandeloylglutathione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q12320

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

substrate: S-D-mandeloylglutathione


sequence_source: UniProt REST direct lookup 2026-06-16, accession Q05584


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: S-D-lactoylglutathione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q8ZRM2

proof_lines: enzyme obtained from minimal medium supplemented with Fe2+

proof_lines: enzyme obtained from minimal medium supplemented with Zn2+

substrate: S-D-lactoylglutathione


organism: Salmonella typhimurium


organism: Shouchella lehensis


organism: Trypanosoma brucei

substrate_name: bis-(lactoyl)trypanothione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q6KF36

proof_lines:
pH 7.2, 25°C
recombinant enzyme, pH 7.2, 25°C
above, recombinant enzyme, pH 7.2, 25°C

substrate: bis-(lactoyl)trypanothione


substrate_name: S-hydroxyglutaryltrypanothione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q581U6

substrate: S-hydroxyglutaryltrypanothione


enzyme_display_name: dGTPase

substrate_name: dGTP

sequence_source: UniProt REST direct lookup 2026-06-16, accession P15723

enzyme: dGTPase

substrate: dGTP


substrate_name: Unknown

substrate: Unknown


organism: Leeuwenhoekiella blandensis

sequence_source: UniProt REST direct lookup 2026-06-16, accession A3XHN1

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


enzyme_display_name: chymase

organism: Cavia porcellus

enzyme: chymase


sequence_source: UniProtKB:P77488 direct accession lookup

column_label: Table 1: Substrate specificity of nitroso substrates (Chembiochem 2013, volume 14, issue 11, pages 1309-1315); printed column heads Substrate | kcat (min^-1) | KM (uM) | kcat/KM, x 10^4 (M^-1 min^-1). Table 1, nitroso substrate row 4; column kcat (min^-1) = 0.9; column KM (uM) = 54; column kcat/KM, x 10^4 (M^-1 min^-1) = 1.7. captured primary segment: Table 1, nitroso substrate 4 | E. coli DXP synthase | kcat 0.9 min^-1 | KM 54 uM | kcat/KM 1.7 x 10^4 M^-1 min^-1 | 100 mM HEPES, pH 8.0, 37 C

normalized_value_unit_evidence: Km: printed Table 1 cell 54 uM; 54 / 1000 = 0.054 mM; the exported value is 0.054 mM. kcat: printed Table 1 cell 0.9 min^-1; 1 min^-1 is 1/60 s^-1, so 0.9 / 60 = 0.015 s^(-1); the exported value is 0.015 s^(-1). kcat/Km: printed Table 1 cell 1.7 x 10^4 M^-1 min^-1; 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1, so 17000 / 60000 = 0.2833333333333333 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.015 / 0.054 = 0.2777777777777778 s^-1 mM^-1, the exported value, and 0.9 / 0.054 = 16.666667 min^-1 mM^-1, that is 1.6666667 x 10^4 M^-1 min^-1, which at the two printed digits of the efficiency column is the printed cell 1.7 x 10^4 M^-1 min^-1.

raw_value_unit_evidence: Table 1, nitroso substrate row 4: kcat = 0.9 min^-1; KM = 54 uM; printed kcat/KM = 1.7 x 10^4 M^-1 min^-1.

row_label: Table 1, nitroso substrate row 4


column_label: Table 1: Substrate specificity of nitroso substrates (Chembiochem 2013, volume 14, issue 11, pages 1309-1315); printed column heads Substrate | kcat (min^-1) | KM (uM) | kcat/KM, x 10^4 (M^-1 min^-1). Table 1, nitroso substrate row 3; column kcat (min^-1) = 36; column KM (uM) = 99; column kcat/KM, x 10^4 (M^-1 min^-1) = 36. captured primary segment: Table 1, nitroso substrate 3 | E. coli DXP synthase | kcat 36 min^-1 | KM 99 uM | kcat/KM 36 x 10^4 M^-1 min^-1 | 100 mM HEPES, pH 8.0, 37 C

normalized_value_unit_evidence: Km: printed Table 1 cell 99 uM; 99 / 1000 = 0.099 mM; the exported value is 0.099 mM. kcat: printed Table 1 cell 36 min^-1; 1 min^-1 is 1/60 s^-1, so 36 / 60 = 0.6 s^(-1); the exported value is 0.6 s^(-1). kcat/Km: printed Table 1 cell 36 x 10^4 M^-1 min^-1; 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1, so 360000 / 60000 = 6.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.6 / 0.099 = 6.06060606060606 s^-1 mM^-1, the exported value, and 36 / 0.099 = 363.63636 min^-1 mM^-1, that is 36.363636 x 10^4 M^-1 min^-1, which at the two printed digits of the efficiency column is the printed cell 36 x 10^4 M^-1 min^-1.

raw_value_unit_evidence: Table 1, nitroso substrate row 3: kcat = 36 min^-1; KM = 99 uM; printed kcat/KM = 36 x 10^4 M^-1 min^-1.

row_label: Table 1, nitroso substrate row 3


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77488 direct accession lookup; variant sequence reconstructed from canonical sequence by applying R478A and applied mutation signature R478A to reconstruct the assayed variant sequence.


substrate_name: D-glyceraldehyde 3-phosphate; 1-methyl-2-nitrosobenzene; 6-bromo-1-nitrosonaphthalen-2-ol; 6-hydroxy-5-nitrosonaphthalene-2-sulfonamide; 1-nitrosonaphthalen-2-ol; N,N-dimethyl-4-nitrosoaniline; 2-hydroxy-4,6-dinitrobenzaldehyde; 7-methoxy-1-nitrosonaphthalen-2-ol; 3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole; pyruvate; D-glyceraldehyde

sequence_source: UniProtKB:P77488 direct accession lookup; canonical accession sequence recorded as identity context

proof_lines: pH 8, temperature not specified in the publication


substrate_name: pyruvate; D-glyceraldehyde 3-phosphate

sequence_source: UniProtKB:P9WNS3 direct accession lookup

proof_lines: wild-type, pH 8.0, temperature not specified in the publication

substrate: pyruvate; D-glyceraldehyde 3-phosphate


substrate_name: D-glyceraldehyde 3-phosphate; pyruvate

sequence_source: UniProtKB:P9WNS3 canonical accession context only; selected source note does not provide a coordinate-validated variant sequence.

proof_lines: mutant lacking loop 190-234, pH 8.0, temperature not specified in the publication

substrate: D-glyceraldehyde 3-phosphate; pyruvate


organism: Plasmodium vivax

sequence_source: UniProtKB:A5K817 direct accession lookup; canonical accession sequence recorded as identity context

proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9KGU7 direct accession lookup; canonical accession sequence recorded as identity context


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9KGU7 direct accession lookup; variant sequence reconstructed from canonical sequence by applying R106A and applied mutation signature R106A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9KGU7 direct accession lookup


organism: Homo sapiens

substrate_name: S-Glycolylglutathione

substrate: S-Glycolylglutathione


substrate_name: (S)-S-Glyceroylglutathione

substrate: (S)-S-Glyceroylglutathione


substrate_name: S-mandeloylglutathione

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

proof_lines:
enzyme from erythrocytes
recombinant enzyme

substrate: S-mandeloylglutathione


substrate_name: (R)-S-Mandeloylglutathione

substrate: (R)-S-Mandeloylglutathione


organism: Leishmania donovani

substrate_name: mono-(lactoyl)trypanothione

substrate: mono-(lactoyl)trypanothione


organism: Leishmania infantum

substrate_name: S-D-lactoyltrypanothione

proof_lines: wild type protein, no activity observed with S-D-lactoylglutathione, pH not specified in the publication, temperature not specified in the publication

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

substrate: S-D-lactoyltrypanothione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y291R/C294K to reconstruct the assayed variant sequence.

proof_lines: Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication


organism: Mus musculus

substrate_name: (R)-S-Lactoylglutathione

substrate: (R)-S-Lactoylglutathione


organism: Nostoc sp. PCC 7120 = FACHB-418

proof_lines:
pH 7.5, 25°C
at pH 7.5 and 25°C


organism: Oryza sativa


organism: Plasmodium falciparum


substrate_name: S-Lactoylglutathione

substrate: S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y185F to reconstruct the assayed variant sequence.


enzyme_display_name: arginine deiminase

organism: Enterococcus faecalis

substrate_name: L-arginine

enzyme: arginine deiminase

substrate: L-arginine


substrate_name: L-Arginine

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

substrate: L-Arginine


proof_lines: pH 6.0, 45°C, mutant enzyme R15K/F269Y/G292P


organism: Giardia duodenalis

substrate_name: L-arginine ethyl ester

sequence_source: UniProtKB Q27657 direct lookup on 2026-06-16; unreviewed TrEMBL entry Q27657_GIAIN for Giardia intestinalis/Giardia lamblia; EC 3.5.3.6.

substrate: L-arginine ethyl ester


organism: Giardia intestinalis


substrate_name: Nomega-amino-L-arginine

substrate: Nomega-amino-L-arginine


organism: Halothermothrix orenii

sequence_source: UniProtKB B8D2J5 direct lookup on 2026-06-16; reviewed Swiss-Prot entry ARCA_HALOH for Halothermothrix orenii strain H 168/OCM 544/DSM 9562; EC 3.5.3.6.


substrate_name: N-alpha-benzoyl-L-arginine ethyl ester

substrate: N-alpha-benzoyl-L-arginine ethyl ester


enzyme_display_name: cathepsin K

sequence_source: UniProtKB REST direct lookup P43235 (UniProtKB reviewed (Swiss-Prot))

enzyme: cathepsin K


proof_lines:
at pH 5.5 and 28°C
at pH 5.5 and 37°C
pH 7.0, 37°C, recombinant enzyme


organism: Rattus norvegicus

sequence_source: UniProtKB REST direct lookup O35186 (UniProtKB reviewed (Swiss-Prot))

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


proof_lines: pH 7.0, 37°C, recombinant mutant S134A/V160L


substrate_name: Abz-HPGGPQ-(3 NO2-Tyr)

proof_lines:
at pH 5.5 and 28°C
pH 5.5, 28°C

substrate: Abz-HPGGPQ-(3 NO2-Tyr)


enzyme_display_name: deaminated glutathione amidase

organism: Arabidopsis thaliana

sequence_source: UniProtKB REST direct lookup Q94JV5 (UniProtKB reviewed (Swiss-Prot))

enzyme: deaminated glutathione amidase


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB REST direct lookup P47016 (UniProtKB reviewed (Swiss-Prot))

proof_lines:
pH 8.5, 30°C
Raw SKiD Env: Temp=30°C, pH=8.5


enzyme_display_name: glutathionylspermidine amidase

organism: Trypanosoma brucei

substrate_name: Glutathionylspermidine

sequence_source: UniProtKB REST direct lookup Q8IEX1 (UniProtKB unreviewed (TrEMBL))

enzyme: glutathionylspermidine amidase

substrate: Glutathionylspermidine


organism: Cavia porcellus


substrate_name: Neurotensin

substrate: Neurotensin


substrate_name: Angiotensin I

substrate: Angiotensin I


enzyme_display_name: tryptase

organism: Equus caballus

substrate_name: N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide

enzyme: tryptase

substrate: N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide


organism: Homo sapiens


proof_lines: mutant enzyme I99C/Y75A/Y37bA, at pH 6.8 and 25°C

proof_lines: mutant enzyme I99C*/Y75A/Y37bA, at pH 6.8 and 25°C


organism: Pseudomonas aeruginosa

substrate_name: L-Arg

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature E224A to reconstruct the assayed variant sequence.

substrate: L-Arg


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R401L to reconstruct the assayed variant sequence.


substrate_name: N(omega)-amino-L-Arginine

sequence_source: UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json)

substrate: N(omega)-amino-L-Arginine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R243K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R185L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R243L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R185A to reconstruct the assayed variant sequence.


substrate_name: Nomega-amino-Arg

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

substrate: Nomega-amino-Arg


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R401A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature E224D to reconstruct the assayed variant sequence.


substrate_name: N(omega)-methyl-L-Arginine

smiles: CN=C(N)NCCCC(N)C(=O)O

substrate: N(omega)-methyl-L-Arginine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R243A to reconstruct the assayed variant sequence.


proof_lines:
at pH 5.6 and 25°C
pH 5.6, 25°C
Raw SKiD Env: Temp=25°C, pH=5.6


organism: Pseudomonas plecoglossicida

sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct accession lookup (https://rest.uniprot.org/uniprotkb/A7LKB0.json) and applied mutation signature K30R/C37R/L148P/V291L to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme K30R/C37R/L148P/V291L


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct accession lookup (https://rest.uniprot.org/uniprotkb/A7LKB0.json) and applied mutation signature K30R/C37R/G129S/L148P/V291L to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme K30R/C37R/G129S/L148P/V291L


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct accession lookup (https://rest.uniprot.org/uniprotkb/A7LKB0.json) and applied mutation signature K5T/D38H/D44E/A128T/E296K/H404R to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme K5T/D38H/D44E/A128T/E296K/H404R


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct entry plus reconstructed A128T/I410L substitutions and applied mutation signature A128T/I410L to reconstruct the assayed variant sequence.


proof_lines: pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K


organism: Pseudomonas putida

sequence_source: UniProtKB:Q88P52 direct entry

proof_lines: pH and temperature not specified in the publication


organism: Streptococcus pyogenes

sequence_source: UniProtKB:B5XMC3 direct entry


enzyme_display_name: 2,3-epoxybenzoyl-CoA dihydrolase

organism: Aromatoleum evansii

sequence_source: UniProtKB:Q84HH6 direct entry

assay_conditions_summary: cofactor CoA

enzyme: 2,3-epoxybenzoyl-CoA dihydrolase


organism: Azoarcus evansii

assay_conditions_summary: pH 9; 295.15 K; cofactor CoA


enzyme_display_name: L-threo-3-deoxy-hexylosonate aldolase

organism: Trichoderma reesei

substrate_name: pyruvate

sequence_source: UniProtKB:A6Y9S5 direct entry

enzyme: L-threo-3-deoxy-hexylosonate aldolase

substrate: pyruvate


substrate_name: L-Glyceraldehyde

substrate: L-Glyceraldehyde


enzyme_display_name: indole-3-glycerol-phosphate lyase

organism: Oryza sativa

sequence_source: UniProtKB:Q7Y1I9 direct entry

enzyme: indole-3-glycerol-phosphate lyase


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProt REST Q2HYA0


organism: Metapseudomonas furukawaii

sequence_source: UniProt REST A0AAD1C5K5


organism: Mycoplasma arthritidis

sequence_source: UniProt REST Q9RND4


organism: Mycoplasmopsis arginini

sequence_source: UniProt REST P23793


sequence_variant_note: Resolved canonical sequence from UniProt REST P13981 with N160A reconstruction and applied mutation signature N160A to reconstruct the assayed variant sequence.


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

organism: Rhodobacter capsulatus

proof_lines: pH 7.4, 37°C, cosubstrate: D-glyceraldehyde 3-phosphate

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


organism: Unknown

substrate_name: Unknown

substrate: Unknown


organism: Arabidopsis thaliana

substrate_name: S-D-mandeloylglutathione

proof_lines: recombinant cytosolic isozyme, minimal medium, pH 7.2, 25°C

proof_lines: pH 7.2, 25°C, growth on minimal medium without added metal ion

proof_lines: recombinant cytosolic isozyme, medium with Zn added, pH 7.2, 25°C

substrate: S-D-mandeloylglutathione


organism: Bos taurus

proof_lines: mitochondrial isozyme, pH 7.2, 25°C, in presence of cardiolipin

proof_lines: mitochondrial isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid


organism: Homo sapiens

proof_lines:
enzyme from brain
enzyme from liver
brain


substrate_name: S-D-lactoylglutathione

substrate: S-D-lactoylglutathione


organism: Cavia porcellus

substrate_name: Benzyloxycarbonyl-Gln-Gly

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

substrate: Benzyloxycarbonyl-Gln-Gly


sequence_source: UniProtKB:H0VXN6 direct REST lookup 2026-06-16


substrate_name: Z-Glu(HMC)-Gly-OH

substrate: Z-Glu(HMC)-Gly-OH


substrate_name: Z-Glu(HC)-Gly-OH

substrate: Z-Glu(HC)-Gly-OH


proof_lines: pH 6.5, 30°C, with/versus substrate Z-Glu(HMC)-Gly-OH


substrate_name: pentylamine

sequence_source: UniProtKB:A0A286XL02 direct REST lookup 2026-06-16

smiles: CCCCCN

substrate: pentylamine


substrate_name: N,N'-dimethyl casein glutamine

sequence_source: UniProtKB:P21980 direct REST lookup 2026-06-16

proof_lines: pH 7.5, 37°C, recombinant TG2 without DNAJA1

proof_lines: 0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C

substrate: N,N'-dimethyl casein glutamine


organism: Pacifastacus leniusculus

sequence_source: UniProtKB:Q964D3 direct REST lookup 2026-06-16


organism: Paracentrotus lividus

substrate_name: GTP

sequence_source: UniProtKB:Q8T316 direct REST lookup 2026-06-16

substrate: GTP


organism: Streptomyces cinnamoneus

substrate_name: L-lysine

sequence_source: UniProtKB:Q8GR90 direct REST lookup 2026-06-16

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

substrate: L-lysine


organism: Streptomyces hygroscopicus

substrate_name: N-Cbz-Gln-Gly

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

proof_lines: mutant enzyme N160Q/N355Q, at pH 6.0 and 37°C

substrate: N-Cbz-Gln-Gly


sequence_source: UniProtKB Q7Y1I9 REST lookup


organism: Zea mays

substrate_name: indole-3-glycerol phosphate

sequence_source: UniProtKB Q9FQ77 REST lookup

substrate: indole-3-glycerol phosphate


sequence_source: UniProtKB B2Y0K4 REST lookup


substrate_name: (3-Indolyl)-glycerol phosphate

sequence_source: UniProtKB P42390 REST lookup

substrate: (3-Indolyl)-glycerol phosphate


enzyme_display_name: (R)-2-methylmalate dehydratase

organism: Methanocaldococcus jannaschii

substrate_name: D-Citramalate

enzyme: (R)-2-methylmalate dehydratase

substrate: D-Citramalate


sequence_source: UniProt REST P43235 FASTA direct check


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

assay_conditions_summary: pH 5.5; 301.15 K; buffer 100 mM sodium acetate

proof_lines: mutant enzyme K9E/N190M/K191G/L195K , in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C

proof_lines: mutant enzyme K9E/N190M/K191G/L195K, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: wild type enzyme, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: mutant enzyme K9E, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: mutant enzyme N190M/K191G/L195K, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: mutant enzyme K9E/I171E/Q172S/N190M/K191G/L195K, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


organism: Pseudomonas plecoglossicida

substrate_name: L-arginine

sequence_source: UniProt REST A7LKB0 FASTA direct check

substrate: L-arginine


proof_lines: pH 7.4, 37°C, mutant enzyme A128T/H404/I410L


substrate_name: L-Arginine

substrate: L-Arginine


organism: Escherichia coli (strain K12)

substrate_name: lauroyl-ACP

substrate: lauroyl-ACP


organism: Cavia cutleri

substrate_name: serotonin (for protein-glutamine serotonyltransferase activity)


substrate_name: PATH

substrate: PATH


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

substrate_name: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)


organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


substrate: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)


enzyme_display_name: sedoheptulokinase

substrate_name: sedoheptulose

enzyme: sedoheptulokinase

substrate: sedoheptulose


organism: Mus musculus


enzyme_display_name: CTP-dependent riboflavin kinase

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

substrate_name: riboflavin

enzyme: CTP-dependent riboflavin kinase

substrate: riboflavin


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

substrate_name: GTP (in the presence of PhnI alone)

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 1.4 sec(-1) for ATP hydrolysis in the presence of PhnI alone, and 20 sec(-1) for RPnTP synthesis from ATP in the presence of PhnI, PhnG, PhnH and PhnL.

substrate: GTP (in the presence of PhnI alone)


enzyme_display_name: (3S)-malyl-CoA thioesterase

substrate_name: (3S)-citramalyl-CoA (for citramalyl-CoA lyase activity)

proof_lines: kcat is 0.12 sec(-1) for malate synthase reaction (PubMed:24334609). kcat is 0.09 sec(-1) for beta-methylmalate synthase reaction (PubMed:24334609). kcat is 0.135 sec(-1) for beta-methylmalate synthase reaction (PubMed:29056341). kcat is 0.

enzyme: (3S)-malyl-CoA thioesterase


enzyme_display_name: hydroxyacylglutathione hydrolase

substrate_name: (R)-S-lactoylglutathione

proof_lines: kcat is 53 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione (PubMed:17196158). kcat is 15.6 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione (PubMed:25670698).

enzyme: hydroxyacylglutathione hydrolase

substrate: (R)-S-lactoylglutathione


proof_lines: kcat is 0.9 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 979 sec(-1) with (R)-S-lactoylglutathione as substrate and 35.1 sec(-1) with (R)-S-mandeloylglutathione as substrate.


proof_lines: kcat is 605 sec(-1) with (R)-S-lactoylglutathione as substrate and 38.1 sec(-1) with (R)-S-mandeloylglutathione as substrate.


substrate_name: ATP (at pH 6.8)

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: kcat is 7 sec(-1) for Gsp synthetase activity at pH 6.8 and 2.1 sec(-1) for Gsp amidase activity at pH 7.5.

substrate: ATP (at pH 6.8)


organism: Aromatoleum evansii

proof_lines: The substrate was earlier believed to be 2,3-dihydro-2,3-dihydroxybenzoyl-CoA but it has later been shown to be the epoxide as the substrate was enzymatically produced by BoxAB.


substrate_name: indole-3-glycerol phosphate

proof_lines: kcat is 0.02 sec(-1) with indole-3-glycerol phosphate as substrate.


enzyme_display_name: L-methionine (S)-S-oxide reductase

organism: Saccharomyces cerevisiae

substrate_name: L-(-)-methionine S-oxide

enzyme: L-methionine (S)-S-oxide reductase

substrate: L-(-)-methionine S-oxide


organism: Agrobacterium tumefaciens

substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Deinococcus radiodurans


substrate_name: pyruvate

substrate: pyruvate


proof_lines: pH and temperature not specified in the publication


organism: Escherichia coli

proof_lines:
pH 8.0, 37°C
Ki above 0.2 mM, at pH 8.0 and 37°C
Ki above 0.1 mM, at pH 8.0 and 37°C


substrate_name: N-Cbz-Gln-Gly

substrate: N-Cbz-Gln-Gly


organism: Streptomyces mobaraensis

substrate_name: Z-Gln-Gly

sequence_source: UniProtKB reviewed entry P81453, direct REST lookup on 2026-06-16

substrate: Z-Gln-Gly


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P81453, direct REST lookup on 2026-06-16 and applied mutation signature S2P with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant S2P, pH 7.2, 37°C
recombinant mutant S2P, pH 6.0, 37°C


proof_lines: recombinant wild-type enzyme, pH 7.2, 37°C

proof_lines: recombinant wild-type enzyme, pH 6.0, 37°C

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


substrate_name: CBZ-Gln-Gly-OH

substrate: CBZ-Gln-Gly-OH


proof_lines: pH 8.0, 37°C, recombinant chimeric mutant


substrate_name: N-CBZ-Glu-Gly

substrate: N-CBZ-Glu-Gly


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


organism: Homo sapiens

sequence_source: UniProtKB reviewed entry P43235, direct REST lookup on 2026-06-16

sequence_variant_note: Mutation signature K9E/I171E/Q172S/N190M/K191G/L195K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K9E/N190M/K191G/L195K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K9E/I171E/Q172S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 5.5; buffer 100 mM sodium acetate

proof_lines: mutant enzyme K9E/I171E/Q172S, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


enzyme_display_name: nicotinamidase

substrate_name: nicotinamide

sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature D51A and applied mutation signature D51A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0024 mM, mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C

proof_lines: kcat/Km above 8.3 (1/sec*mM), mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C

enzyme: nicotinamidase

substrate: nicotinamide


sequence_source: UniProtKB:P53184 reviewed canonical FASTA direct lookup

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; cofactor NADPH

column_label: Table 4 (Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates), body row 'nicotinamide': column 'kcat (s-1)' = 0.69; column 'Km (uM)' = 9.6; column 'kcat/Km (M-1 s-1)' = 7.2 x 10^4. The number printed after the plus/minus sign beside the kcat and Km cells of this line is the printed uncertainty and is not an exported metric. The 15N KIE and 13C KIE columns of the same line print 1.0122 and 1.0125, which are isotope effects and not kinetic metric fields the export schema carries.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.69 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.69 s^(-1). Km: printed Table 4 cell 9.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 9.6 / 1000 = 0.0096 mM. kcat/Km: printed Table 4 cell 7.2 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.2 x 10^4 / 1000 = 72.0 s^(-1)*mM^(-1). The exported values are kcat 2.56 s^(-1) and Km 0.0096 mM.

raw_value_unit_evidence: Table 4, body row 'nicotinamide': kcat = 0.69 s-1; Km = 9.6 uM; printed kcat/Km = 7.2 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 4, row nicotinamide

table_label: Table 4: Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates (Biochemistry 2012, 51(1):243-256). Printed column heads: Substrate; Structure; kcat (s-1); Km (uM); kcat/Km (M-1 s-1); 15N KIE; 13C KIE.