enzyme_display_name: 7-deoxyloganetin glucosyltransferase

organism: Catharanthus roseus

proof_lines: kcat is 0.0355 sec(-1) for 7-deoxyloganetin. kcat is 0.0320 sec(-1) for UPD-glucose.

enzyme: 7-deoxyloganetin glucosyltransferase


organism: Gardenia jasminoides

substrate_name: genipin

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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.

proof_lines: kcat is 1.04 sec(-1) for genipin. kcat is 0.13 sec(-1) for 7-deoxyloganetin. kcat is 0.16 sec(-1) for UPD-glucose.

substrate: genipin

source: uniprot


substrate_name: UDP-alpha-D-glucose

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProtKB:F8WLS6 direct accession lookup on 2026-06-27 (UniProtKB reviewed (Swiss-Prot); length 487; CRC64 A6E423A362B9E0CF)

data_origin: experimental

substrate: UDP-alpha-D-glucose

status: unverified

source: oed


source_db: brenda

source: brenda


sequence_source: UniProtKB:F8WKW5 direct accession lookup on 2026-06-27 (UniProtKB unreviewed (TrEMBL); length 493; CRC64 4110C8F69F3661CB)


enzyme_display_name: tagatose-6-phosphate kinase

organism: Unknown

substrate_name: ATP

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

assay_conditions_summary: cofactor ATP

enzyme: tagatose-6-phosphate kinase

substrate: ATP


organism: Lactococcus lactis subsp. lactis

substrate_name: ATP; D-Tagatose 6-phosphate

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

substrate: ATP; D-Tagatose 6-phosphate


organism: Staphylococcus aureus

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


enzyme_display_name: beta-N-acetylgalactosaminidase

organism: Paenibacillus sp.

sequence_source: UniProtKB:E9RH20 REST lookup on 2026-06-27 returned inactive/deleted record without replacement sequence

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

mutation_type: substitution

enzyme: beta-N-acetylgalactosaminidase


km_display: Not reported


organism: Bacillus sp. (in: firmicutes)


organism: Bos taurus


organism: Rattus norvegicus


organism: Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc)

substrate_name: pNP-GlcNAc (at pH 7.0 and 37 degrees Celsius)

proof_lines: kcat is 51.39 sec(-1) and kcat/KM is 1.73 M(-1)sec(-1) with pNP-GlcNAc as substrate.


enzyme_display_name: adrenodoxin-NADP(+) reductase

organism: Mycobacterium tuberculosis

substrate_name: NADH

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADPH

proof_lines: diaphorase activity with ferricyanide, pH 7.2, 30°C

enzyme: adrenodoxin-NADP(+) reductase

substrate: NADH


enzyme_display_name: 5-aminolevulinate synthase

organism: Homo sapiens

substrate_name: succinyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: 5-aminolevulinate synthase

substrate: succinyl-CoA


substrate_name: glycine

substrate: glycine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: succinyl-CoA; glycine

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

ki_unit: mM

sequence_source: UniProtKB:P22557 direct REST lookup on 2026-06-27

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: apparent value, pH and temperature not specified in the publication

source_databases_merged: brenda skid

substrate: succinyl-CoA; glycine


organism: Mus musculus

sequence_source: UniProtKB:P08680 direct REST lookup on 2026-06-27; canonical sequence retained as context only

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 7.5; 291.15 K; cofactor CoA


sequence_source: UniProtKB:P08680 direct REST lookup on 2026-06-27


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Rhodobacter capsulatus

substrate_name: glycine; succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P18079 direct REST lookup on 2026-06-27 plus explicit residue substitutions I325M/V390Y/H391I and applied mutation signature I325M/V390Y/H391I to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, mutant enzyme I325M/V390Y/H391I

substrate: glycine; succinyl-CoA


enzyme_display_name: glutamine kinase

organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: L-glutamine (at pH 8.0 and 25 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 2.5 sec(-1) with L-glutamine as substrate (PubMed:28650156, PubMed:30142271). kcat is 1.5 sec(-1) with D-glutamine as substrate. kcat is 2.1 sec(-1) with gamma-L-glutamyl hydroxamate as substrate. kcat is 0.41 sec(-1) with gamma-L-g

enzyme: glutamine kinase


organism: Campylobacter jejuni

sequence_source: UniProtKB Q0P8J6; paper-linked Cj1418c target from PMID 28650156

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


substrate_name: L-Glutamine; ATP; H2O

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

sequence_source: UniProtKB reviewed accession Q0P8J6; direct lookup 2026-06-27

substrate: L-Glutamine; ATP; H2O


substrate_name: D-Glutamine

substrate: D-Glutamine


substrate_name: gamma-L-glutamyl hydrazide

substrate: gamma-L-glutamyl hydrazide


substrate_name: L-glutamine

assay_conditions_summary: pH 8; 355.15 K; cofactor ATP

substrate: L-glutamine


substrate_name: gamma-L-glutamyl hydroxamate

substrate: gamma-L-glutamyl hydroxamate


enzyme_display_name: trimethyltridecatetraene synthase

organism: Zea mays

sequence_source: UniProtKB reviewed accession A0A1D6F9Y9 (C92C6_MAIZE), fetched during targeted PMID/gene follow-up

proof_lines: pH and temperature not specified in the publication

enzyme: trimethyltridecatetraene synthase


organism: Arabidopsis thaliana

substrate_name: (6E,10E)-Geranyllinalool; O2; NADPH; H+

assay_conditions_summary: cofactor NADPH

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

substrate: (6E,10E)-Geranyllinalool; O2; NADPH; H+


substrate_name: H+; NADPH; O2; (6E,10E)-Geranyllinalool

substrate: H+; NADPH; O2; (6E,10E)-Geranyllinalool


enzyme_display_name: vancomycin aglycone glucosyltransferase

organism: Amycolatopsis orientalis

substrate_name: UDP-alpha-D-glucose

sequence_source: UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1

enzyme: vancomycin aglycone glucosyltransferase


substrate_name: vancomycin aglycone

substrate: vancomycin aglycone


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1 and applied mutation signature H125A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H125A, pH and temperature not specified in the publication

substrate: UDP-alpha-D-glucose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1 and applied mutation signature D332A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D332A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1 and applied mutation signature D13A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D13A, pH and temperature not specified in the publication


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


substrate_name: UDP-glucose

substrate: UDP-glucose


enzyme_display_name: dehydrogluconokinase

organism: Klebsiella aerogenes

enzyme: dehydrogluconokinase


organism: Cupriavidus necator

substrate_name: ATP

sequence_source: UniProtKB:Q0K080, cross-checked against NCBI YP_841324.1 and WP_010810288.1 on 2026-06-27

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: ATP; 2-Dehydro-D-gluconate

proof_lines: pH 8.0, temperature not specified in the publication

substrate: ATP; 2-Dehydro-D-gluconate


enzyme_display_name: 2-aminobenzoylacetyl-CoA thioesterase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: S-ethyl-acetothioacetate

proof_lines: kcat is 0.85 sec(-1) with S-ethyl-acetothioacetate as substrate. kcat is 0.36 sec(-1) with acetoacetyl-CoA as substrate. kcat is 0.022 sec(-1) with cysteamine-S-phosphate as substrate (PubMed:25960261). kcat is 7.2 min(-1) with S-(4-nitrobe

enzyme: 2-aminobenzoylacetyl-CoA thioesterase

substrate: S-ethyl-acetothioacetate


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB direct lookup for reviewed accession P20581

proof_lines: wild-type, pH 8.5, 25°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup for reviewed accession P20581 plus local E182A substitution reconstruction and applied mutation signature E182A to reconstruct the assayed variant sequence.

proof_lines: mutant E182A, pH 8.5, 25°C, presence of Mn2+


substrate_name: acetoacetyl-CoA

sequence_source: UniProtKB direct lookup for unreviewed accession A0A0H2Z6F6

assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA

proof_lines:
pH 8.2, 30°C
Raw SKiD Env: Temp=30°C, pH=8.2

substrate: acetoacetyl-CoA


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


enzyme_display_name: L-galactose 1-phosphate phosphatase

substrate_name: D-myoinositol 3-phosphate

enzyme: L-galactose 1-phosphate phosphatase

substrate: D-myoinositol 3-phosphate


organism: Actinidia deliciosa

substrate_name: L-Galactose 1-phosphate; H2O

sequence_source: UniProtKB REST direct accession lookup Q5U789 on 2026-06-27; active TrEMBL entry Q5U789_ACTDE.

substrate: L-Galactose 1-phosphate; H2O


substrate_name: beta-L-galactose 1-phosphate

proof_lines: pH 7.0, 30°C, 1.8 mM Mg2+, native enzyme

substrate: beta-L-galactose 1-phosphate


sequence_source: UniProtKB REST direct accession lookup Q9M8S8 on 2026-06-27; reviewed Swiss-Prot entry VTC4_ARATH.


sequence_source: UniProtKB reviewed accession P9WNH5 / HSAD_MYCTU direct lookup


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (at pH 7.5 and at 25 degrees Celsius)


assay_conditions_summary: pH 7.4; 298.15 K; buffer 100 mM of phosphate

proof_lines: apparent value, in 100 mM of phosphate buffer (pH 7.4) with 20 mM NaCl, temperature not specified in the publication

proof_lines: in 20 mM HEPES, 80 mM NaCl, at pH 8.0 and 25°C


proof_lines: wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C


proof_lines: mutant enzyme S114A, in 100 mM potassium phosphate, pH 7.5, at 25°C


organism: Gallus gallus

assay_conditions_summary: pH 8


organism: Treponema denticola

sequence_source: UniProtKB reviewed accession Q73PV9 / PURE_TREDE, direct REST lookup on 2026-06-27


substrate_name: 4-carboxy-5-aminoimidazole ribonucleotide; CO2; 5-aminoimidazole ribonucleotide

source_db: brenda;skid

proof_lines:
50 mM Tris-HCl (pH 8.0), at 30°C
50 mM Tris-HCl (pH 8.0), at 10°C
Raw SKiD Env: Temp=30°C, pH=8

source: brenda;skid


organism: Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)

substrate_name: CO(2) (at 10 degrees Celsius)

substrate: CO(2) (at 10 degrees Celsius)


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,4-lactone-forming)

organism: Haloarcula marismortui

substrate_name: D-ribose

substrate: D-ribose


substrate_name: D-Xylose

enzyme: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,4-lactone-forming)

substrate: D-Xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-ribose; D-xylose; D-glucose; NAD+; NADP+

assay_conditions_summary: pH 8.3; 310.15 K; cofactor NADP+


organism: Haloferax volcanii

substrate_name: NAD+; D-xylose; NADP+; D-glucose

assay_conditions_summary: pH 7.5; 315.15 K; cofactor NADP+

substrate: NAD+; D-xylose; NADP+; D-glucose


organism: Eupatorium cannabinum

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines: NAD+ functions as an enzyme-bound redoxsystem that is reduced in the first and reoxidized in the second part of the overall reaction. It functions as a coenzyme and not a cosubstrate

substrate: NAD+


organism: Senecio vernalis

substrate_name: putrescine

substrate: putrescine


substrate_name: Spermidine

smiles: NCCCCNCCCN

substrate: Spermidine


substrate_name: Putrescine; Spermidine

substrate: Putrescine; Spermidine


substrate_name: Putrescine

smiles: NCCCCN

substrate: Putrescine


enzyme_display_name: tetrahydrocannabinolic acid synthase

organism: Cannabis sativa

substrate_name: cannabigerolate

proof_lines: recombinant enzyme, in 100 mM sodium citrate (pH 5.5), at 30°C

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

enzyme: tetrahydrocannabinolic acid synthase

substrate: cannabigerolate


substrate_name: cannabigerolic acid

proof_lines: kcat is 0.30 sec(-1) for cannabigerolate.

substrate: cannabigerolic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GTB6 and applied mutation signature R110A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GTB6 and applied mutation signature R108A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 5; 303.15 K; buffer 100 mM sodium citrate

proof_lines: mutant enzyme R108A, in 100 mM sodium citrate buffer (pH 5.0), at 30°C


proof_lines: wild type enzyme, in 100 mM sodium citrate buffer (pH 5.0), at 30°C


proof_lines: mutant enzyme R110A, in 100 mM sodium citrate buffer (pH 5.0), at 30°C


enzyme_display_name: sphingomyelin phosphodiesterase D

organism: Corynebacterium pseudotuberculosis

substrate_name: H2O; 1-Oleoylglycerophosphocholine

sequence_source: UniProtKB reviewed accession P20626, fetched by direct accession lookup on 2026-06-27

enzyme: sphingomyelin phosphodiesterase D

substrate: H2O; 1-Oleoylglycerophosphocholine


organism: Loxosceles intermedia

substrate_name: sphingomyelin

sequence_source: UniProtKB reviewed accession P0CE81, fetched by direct accession lookup on 2026-06-27

substrate: sphingomyelin


organism: Loxosceles laeta

sequence_source: UniProtKB reviewed accession Q8I914, fetched by direct accession lookup on 2026-06-27

proof_lines: recombinant enzyme SMase II, in HEPES-buffered saline at 37°C


sequence_source: UniProtKB reviewed accession Q8I912, fetched by direct accession lookup on 2026-06-27

proof_lines: recombinant enzyme SMase I, in HEPES-buffered saline at 37°C

proof_lines: crude enzyme, in HEPES-buffered saline at 37°C


proof_lines:
37°C, pH 7.4, sphingomyelinase P2
at pH 7.4 and 37°C


proof_lines: at 37°C, pH not specified in the publication


organism: Rattus norvegicus


enzyme_display_name: protein arginine phosphatase

substrate_name: [culpeine]-Nomega-phospho-L-arginine

enzyme: protein arginine phosphatase

substrate: [culpeine]-Nomega-phospho-L-arginine


organism: Bacillus subtilis (strain 168)

substrate_name: p-nitrophenyl-phosphate (at 37 degrees Celsius and pH 5.5)

proof_lines: kcat is 0.010 sec(-1) with pNPP as substrate (at 37 degrees Celsius and pH 5.5) (PubMed:15995210). kcat is 0.13 sec(-1) with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242). pNPP is a phosphotyrosine mimicking compound.


organism: Geobacillus stearothermophilus

substrate_name: p-nitrophenyl-phosphate (at 25 degrees Celsius and pH 7.6)

proof_lines: kcat is 1.12 sec(-1) with pNPP as substrate (at 25 degrees Celsius and pH 7.6) (PubMed:23838530) and 3.2 sec(-1) with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242). pNPP is a phosphotyrosine mimicking compound.


organism: Drosophila melanogaster

substrate_name: phospho-L-arginine

sequence_source: UniProtKB Q8ING6, live TrEMBL entry Q8ING6_DROME

substrate: phospho-L-arginine


substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB S0F332, reviewed Swiss-Prot entry PAP_GEOSE

substrate: 4-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB S0F332 plus C14S reconstruction from the source mutation signature and applied mutation signature C14S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB S0F332 plus C14S reconstruction from the source mutation signature


enzyme_display_name: chondroitin 4-sulfotransferase

organism: Homo sapiens

substrate_name: PAPS

enzyme: chondroitin 4-sulfotransferase

substrate: PAPS


proof_lines:
pH 6.8, 37°C, in presence of protamine
pH 6.8, 37°C, in addition of spermine
pH 6.8, 37°C, in addition of Mn2+


mutation_type: deletion

proof_lines: pH 6.8, 37°C, mutant with deletion of C-terminal glycosylation site


substrate_name: 3'-phosphoadenylyl sulfate

sequence_source: UniProtKB reviewed FASTA accession Q9NPF2, retrieved by direct accession lookup on 2026-06-27.

proof_lines: pH 7.0, 37°C, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, recombinant enzyme expressed in Pichia pastoris

substrate: 3'-phosphoadenylyl sulfate


organism: Mus musculus

substrate_name: 3'-Phosphoadenylyl sulfate; Chondroitin

sequence_source: UniProtKB reviewed FASTA accession Q9JME2, retrieved by direct accession lookup on 2026-06-27.

substrate: 3'-Phosphoadenylyl sulfate; Chondroitin


sequence_source: UniProtKB reviewed FASTA accession P69478, retrieved by direct accession lookup on 2026-06-27.


enzyme_display_name: CMP-N-acetylneuraminate monooxygenase

organism: Asterias rubens

substrate_name: CMP-N-acetylneuraminate

proof_lines: pH 6.4, 25°C, soluble form of ferrocytochrome b5

proof_lines: pH 6.4, 25°C, amphiphilic form of ferrocytochrome b5

enzyme: CMP-N-acetylneuraminate monooxygenase

substrate: CMP-N-acetylneuraminate


proof_lines:
pH 7.4, 37°C, soluble system
pH 7.5, 37°C
pH 7.4, 37°C, amphiphilic system


organism: Sus scrofa

proof_lines: pH 7.4, 37°C, reconstituted system consisting of purified hydroxylase, cytochrome b5, cytochrome b5 reductase and catalase

proof_lines: pH 7.4, 37°C, purified hydroxylase in presence of Triton X-100 solubilized microsomes

proof_lines: pH 7.4, 37°C, enzyme from submaxillary gland


substrate_name: CMP-NeuAc

substrate: CMP-NeuAc


substrate_name: H+; O2; Ferrocytochrome b5; CMP-N-acetylneuraminate

sequence_source: UniProtKB Q95V11 reviewed Swiss-Prot entry CMAH_ASTRU, checked 2026-06-27 via UniProt REST


substrate_name: Ferrocytochrome b5; H+; O2; CMP-N-acetylneuraminate

sequence_source: UniProtKB Q61419 reviewed Swiss-Prot entry CMAH_MOUSE, checked 2026-06-27 via UniProt REST

assay_conditions_summary: cofactor NADH


substrate_name: cytochrome b5

proof_lines: Decreased enzyme activity in presence of 100 mM of NaCl.

substrate: cytochrome b5


enzyme_display_name: nucleoside-phosphate kinase

substrate_name: dAMP

proof_lines: isoform AMPK1, in 50 mM Tris/HCl (pH 7.4), 50 mM KCl, 5 mM MgCl2, at 37°C

proof_lines: in Tris-HCl (50 mM, pH 7.4), KCl (50 mM), MgCl2 (5 mM), at 37°C

proof_lines: isoform AMPK2, in 50 mM Tris/HCl (pH 7.4), 50 mM KCl, 5 mM MgCl2, at 37°C

enzyme: nucleoside-phosphate kinase

substrate: dAMP


substrate_name: ATP; AMP

sequence_source: UniProtKB reviewed accession Q5TCS8 direct REST check on 2026-06-27

assay_conditions_summary: cofactor ATP

substrate: ATP; AMP


organism: Gallus gallus

substrate_name: ATP

substrate: ATP


substrate_name: AMP with ATP as phosphate donor

substrate: AMP with ATP as phosphate donor


substrate_name: AMP (with ATP as phosphate donor)

substrate: AMP (with ATP as phosphate donor)


substrate_name: ThDP

assay_conditions_summary: cofactor ADP

substrate: ThDP


substrate_name: O-(alpha-L-iduronic acid 2-sulfate)-(1-4)-D-O-(alpha 2-sulfaminoglucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid 2-sulfate)-D-O-2,5-anhydro-mannitol 6-sulfate

proof_lines:
pH dependent
recombinant protein
in presence of 7 mM NaCl


substrate_name: O-(alpha-L-Idopyranosyluronic acid 2-sulfate)-(1->4)-2,5-anhydro-D-mannitol 6-sulfate; H2O

sequence_source: UniProtKB reviewed accession P22304, direct UniProt REST lookup


verification_status: corrected

status: corrected


substrate_name: sphingomyelin

proof_lines: recombinant enzyme SMase II, in HEPES-buffered saline at 37°C


enzyme_display_name: 2-acylglycerol O-acyltransferase

organism: Arachis hypogaea

substrate_name: oleoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: 2-acylglycerol O-acyltransferase

substrate: oleoyl-CoA


organism: Locusta migratoria


organism: Zonotrichia albicollis

substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: oleoyl-CoA; 1-oleoyl-sn-glycerol

sequence_source: UniProtKB REST exact accession lookup for H9LBH7; TrEMBL entry H9LBH7_ARAHY, sequence version 1, organism Arachis hypogaea.

proof_lines: pH and temperature not specified in the publication

substrate: oleoyl-CoA; 1-oleoyl-sn-glycerol


substrate_name: sn-1-Monooleoylglycerol; Oleoyl-CoA

sequence_source: UniProtKB REST exact accession lookup for Q3SYC2; reviewed Swiss-Prot entry MOGT2_HUMAN, sequence version 2, organism Homo sapiens.

substrate: sn-1-Monooleoylglycerol; Oleoyl-CoA


enzyme_display_name: heparanase

substrate_name: fondaparinux

enzyme: heparanase

substrate: fondaparinux


substrate_name: M09 S05a, a heparin sulfate analog with a nonasaccharide with N-sulfation and a single GlcNS(6S) toward the reducing end


substrate_name: fondaparinux / heparan sulfate disaccharide source labels unresolved

sequence_source: UniProtKB reviewed accession Q9Y251 direct lookup; entry HPSE_HUMAN, Homo sapiens heparanase, EC 3.2.1.166


assay_conditions_summary: pH 5


enzyme_display_name: allantoinase

organism: Phaseolus vulgaris

substrate_name: allantoin

proof_lines: pH 7.8, 40°C, isozyme IsoI, different methods

proof_lines: pH 7.8, 40°C, isozyme IsoII, different methods

enzyme: allantoinase

substrate: allantoin


organism: Unknown

substrate_name: (S)-allantoin

substrate: (S)-allantoin


organism: Cajanus cajan


organism: Escherichia coli

proof_lines:
pH 7.4, 37°C, Zn2+-amended culture
pH 7.4, 37°C, Co2+-amended culture
pH 7.4, 37°C, Ni2+-amended culture


organism: Glycine max

substrate_name: H2O; (S)(+)-Allantoin

substrate: H2O; (S)(+)-Allantoin


organism: Lathyrus sativus


organism: Pseudomonas aeruginosa


organism: Ricinus communis


organism: Salmonella enterica

proof_lines: pH 8.0, 25°C, recombinant enzyme, in presence of phthalimide

proof_lines: pH 8.0, 25°C, recombinant enzyme, in presence of dihydroorotate


organism: Vigna radiata


organism: Vigna unguiculata subsp. cylindrica

proof_lines:
pH 7.5
pH 4


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)

substrate_name: allantoin (at 40 degrees Celsius and pH 8.0)


proof_lines:
Zn2+-activated enzyme, pH 8.0, 25°C
Mn2+-activated enzyme, pH 8.0, 25°C
Ni2+-activated enzyme, pH 8.0, 25°C


organism: Pseudomonas fluorescens

sequence_source: UniProtKB B5L363 FASTA, checked 2026-06-27


sequence_source: UniProtKB REST direct accession check, Q94AP0, 2026-06-27


substrate_name: (S)(+)-Allantoin

substrate: (S)(+)-Allantoin


organism: Bacillus licheniformis

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, L0CR34, with row-specific T155Y reconstruction, 2026-06-27 and applied mutation signature T155Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, L0CR34, with row-specific T155A reconstruction, 2026-06-27 and applied mutation signature T155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, L0CR34, with row-specific S292A reconstruction, 2026-06-27 and applied mutation signature S292A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct accession check, L0CR34, with row-specific S292A reconstruction, 2026-06-27


sequence_source: UniProtKB REST direct accession check, L0CR34, with row-specific T155A reconstruction, 2026-06-27


sequence_source: UniProtKB REST direct accession check, L0CR34, with row-specific T155Y reconstruction, 2026-06-27


sequence_source: UniProtKB REST direct accession check, L0CR34, 2026-06-27

proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme and mutant S292A


substrate_name: H2O; Allantoin

sequence_source: UniProtKB REST direct accession check, P77671, 2026-06-27

substrate: H2O; Allantoin


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, P77671, with row-specific R215K reconstruction, 2026-06-27 and applied mutation signature R215K to reconstruct the assayed variant sequence.

proof_lines: mutant R215K, supplementation with zinc acetate


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

proof_lines: wild-type allantoinase, supplementation with zinc acetate

proof_lines: selenomethionine-substituted wild-type allantoinase, no supplementation with zinc acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, P77671, with row-specific S288D reconstruction, 2026-06-27 and applied mutation signature S288D to reconstruct the assayed variant sequence.

proof_lines: mutant S288D, supplementation with zinc acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, P77671, with row-specific S288V reconstruction, 2026-06-27 and applied mutation signature S288V to reconstruct the assayed variant sequence.

proof_lines: mutant S288V, supplementation with zinc acetate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 11.7 min(-1) for cholesterol as substrate. kcat is 1.5 min(-1) for cholest-4-en-3-one as substrate.


proof_lines: kcat is 84 min(-1) for cholest-4-en-3-one as substrate (PubMed:20843794). kcat is 16.7 min(-1) for cholesterol as substrate (PubMed:20843794). kcat is 0.0062 min(-1) for cholest-4-en-3-one as substrate (PubMed:20889498).


organism: Mycobacterium tuberculosis

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


sequence_source: UniProtKB reviewed accession P9WPL5 direct lookup; UniProtKB ID CP142_MYCTU; CRC64 BCFF3C23ECB5767F

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


organism: Mycolicibacterium smegmatis

sequence_source: UniProtKB reviewed accession A0R4Q6 direct lookup; UniProtKB ID CP142_MYCS2; CRC64 9195ECA2F9D8D509

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


enzyme_display_name: very-long-chain 3-oxoacyl-CoA synthase

organism: Saccharomyces cerevisiae

substrate_name: lauroyl-CoA

assay_conditions_summary: pH 6.7; 303.15 K; cofactor CoA

proof_lines: in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C

enzyme: very-long-chain 3-oxoacyl-CoA synthase

substrate: lauroyl-CoA


organism: Homo sapiens

substrate_name: alpha-Linolenoyl-CoA; Malonyl-CoA

substrate: alpha-Linolenoyl-CoA; Malonyl-CoA


substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 6.8; 310.15 K; cofactor CoA

substrate: palmitoyl-CoA


substrate_name: Malonyl-CoA; Octanoyl-CoA

substrate: Malonyl-CoA; Octanoyl-CoA


substrate_name: hexadecanoyl-CoA (at 37 degrees Celsius and pH 6.8)

assay_conditions_summary: pH 6.8; cofactor CoA


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


enzyme_display_name: inosine kinase

organism: Helianthus tuberosus

substrate_name: Inosine

enzyme: inosine kinase

substrate: Inosine


organism: Limnospira platensis


organism: Mus musculus


substrate_name: guanosine

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

substrate: guanosine


organism: Exiguobacterium acetylicum


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

substrate_name: ATP (at 70 degrees Celsius)

substrate: ATP (at 70 degrees Celsius)


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

substrate_name: guanosine (at pH 8.0 and 22 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 0.072 sec(-1) with ATP and guanosine as substrates. kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1) with ATP and adenosine as substrates. kcat


enzyme_display_name: trehalose 2-sulfotransferase

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

substrate_name: 3'-phosphoadenylyl sulfate

sequence_source: source_record; direct UniProt A0QQ53 FASTA checksum match

proof_lines: kcat is 1.6 sec(-1) (PubMed:15258569). kcat is 134 min(-1) toward trehalose and 96 min(-1) toward PAPS (PubMed:15866533).

enzyme: trehalose 2-sulfotransferase

substrate: 3'-phosphoadenylyl sulfate


sequence_source: Direct UniProtKB lookup for source accession O53699 on 2026-06-27

proof_lines: pH 7.5, 22°C, competitive inhibitor with regard to 3-phosphoadenylyl sulfate

proof_lines: pH 7.5, 22°C, noncompetitive inhibitor with regard to trehalose


substrate_name: alpha,alpha-trehalose

sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup for source accession P84151 plus E36Q substitution reconstructed on 2026-06-27 and applied mutation signature E36Q to reconstruct the assayed variant sequence.

substrate: alpha,alpha-trehalose


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup for source accession P84151 plus E33A substitution reconstructed on 2026-06-27 and applied mutation signature E33A to reconstruct the assayed variant sequence.


sequence_source: Direct UniProtKB lookup for source accession P84151 on 2026-06-27


sequence_source: Direct UniProtKB lookup for source accession P84151 plus E36Q substitution reconstructed on 2026-06-27


sequence_source: Direct UniProtKB lookup for source accession P84151 plus E33A substitution reconstructed on 2026-06-27


organism: Escherichia coli

substrate_name: dATP

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines:
pH 7.2, 30°C, guanosine kinase reaction
pH 7.2, 30°C
pH 7.2, 30°C, inosine kinase reaction

substrate: dATP


organism: Rattus norvegicus


substrate_name: Unknown

substrate: Unknown


organism: Arachis hypogaea

substrate_name: oleoyl-CoA

sequence_source: UniProtKB:H9LBH7 cross-checked against NCBI Protein AEA11209.1 / EMBL JF340215.1

proof_lines: pH and temperature not specified in the publication

substrate: oleoyl-CoA


sequence_source: UniProtKB reviewed accession O53699 direct REST/FASTA lookup on 2026-06-27


enzyme_display_name: succinyl-CoA:mesaconate CoA transferase

organism: Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)

substrate_name: succinyl-CoA (in the presence of 10 mM mesaconate)

enzyme: succinyl-CoA:mesaconate CoA transferase


organism: Haloarcula hispanica

substrate_name: mesaconate

sequence_source: UniProtKB reviewed accession G0HQ31 (MCT_HALHT), fetched via UniProt REST on 2026-06-27

assay_conditions_summary: pH 7.8; 310.15 K; cofactor CoA

substrate: mesaconate


substrate_name: succinyl-CoA

substrate: succinyl-CoA


proof_lines:
37°C, pH 7.8
37°C, pH 7.8, 1 mM succinyl-CoA
37°C, pH 7.8, 5 mM succinyl-CoA


enzyme_display_name: FMN hydrolase

organism: Arabidopsis thaliana

substrate_name: FMN

sequence_source: source_record; direct UniProt accession check for Q84VZ1 matched the selected source sequence

assay_conditions_summary: cofactor FMN

proof_lines: kcat is 0.59 sec(-1) for FMN (PubMed:22002057). kcat is 2.80 sec(-1) for 5-amino-6-(5-phospho-D-ribitylamino)uracil (PubMed:27490826).

enzyme: FMN hydrolase

substrate: FMN


organism: Capra hircus

assay_conditions_summary: pH 5; 323.15 K; cofactor FMN


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

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


assay_conditions_summary: pH 5; 298.15 K; cofactor FAD


substrate_name: riboflavin (at pH 7.5)

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

assay_conditions_summary: pH 7.5; cofactor FMN

substrate: riboflavin (at pH 7.5)


sequence_source: UniProtKB reviewed entry Q84MD8 direct REST/FASTA lookup

assay_conditions_summary: pH 7.5; 303.15 K; cofactor FMN


sequence_source: UniProtKB unreviewed entry F4HQA8 direct REST/FASTA lookup

assay_conditions_summary: pH 8; 303.15 K; cofactor FMN


enzyme_display_name: D-dopachrome decarboxylase

substrate_name: D-dopachrome

enzyme: D-dopachrome decarboxylase

substrate: D-dopachrome


sequence_source: UniProtKB reviewed accession P30046, D-dopachrome decarboxylase, Homo sapiens, EC 4.1.1.84

proof_lines:
pH 6.2, 23°C
Raw SKiD Env: Temp=25°C, pH=6.5


sequence_source: UniProtKB reviewed accession P30046 plus PMID 9480844 P1A mutation context

sequence_variant_note: Mutation signature P1A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB reviewed accession P80254, D-dopachrome decarboxylase, Rattus norvegicus, EC 4.1.1.84


enzyme_display_name: cellobiose phosphorylase

organism: Unknown

substrate_name: cellobiose

enzyme: cellobiose phosphorylase

substrate: cellobiose


organism: Acetivibrio thermocellus

sequence_source: UniProtKB Q8VP44 canonical sequence direct lookup; retrieved 2026-06-27.

proof_lines: synthetic reaction, wild-type, pH 7.5, 45°C

proof_lines: phosphorolytic reaction, wild-type, pH 7.5, 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8VP44 canonical sequence reconstructed with selected mutation signature S497G; retrieved 2026-06-27. and applied mutation signature S497G to reconstruct the assayed variant sequence.

proof_lines: synthetic reaction, mutant S497G, pH 7.5, 45°C

proof_lines: phosphorolytic reaction, mutant S497G, pH 7.5, 50°C


organism: Caldicellulosiruptor bescii

sequence_source: UniProtKB direct lookup B9MNR3 (2026-06-27) returned no live sequence.


organism: Cellulomonas uda

substrate_name: lactose

verification_status: verified

sequence_source: UniProtKB Q7WTR6 canonical sequence direct lookup; retrieved 2026-06-27.

column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'CP', lactose phosphorolysis block: column 'kcat (s^-1)' = 0.109; column 'Km (mM)' = 228; column 'kcat/Km (M^-1 s^-1)' = 0.48.

normalized_value_unit_evidence: kcat: printed Table III cell 0.109 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 0.109 s^(-1). Km: printed Table III cell 228 mM; the column head prints mM, so no unit conversion applies and the paper value is 228.0 mM. kcat/Km: printed Table III cell 0.48 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.48 / 1000 = 0.00048 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row CP (wild-type), lactose phosphorolysis block: kcat = 0.109 s^-1; Km = 228 mM; printed kcat/Km = 0.48 M^-1 s^-1.

row_label: Table III, row CP (wild-type), lactose phosphorolysis columns

substrate: lactose

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q7WTR6 and applied mutation signature T508A/N667T to reconstruct the assayed variant sequence.

column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'LP2', lactose phosphorolysis block: column 'kcat (s^-1)' = 0.53; column 'Km (mM)' = 254; column 'kcat/Km (M^-1 s^-1)' = 2.07.

normalized_value_unit_evidence: kcat: printed Table III cell 0.53 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 0.53 s^(-1). Km: printed Table III cell 254 mM; the column head prints mM, so no unit conversion applies and the paper value is 254.0 mM. kcat/Km: printed Table III cell 2.07 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.07 / 1000 = 0.00207 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row LP2 (T508A/N667T), lactose phosphorolysis block: kcat = 0.53 s^-1; Km = 254 mM; printed kcat/Km = 2.07 M^-1 s^-1.

row_label: Table III, row LP2 (T508A/N667T), lactose phosphorolysis columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature T508I/N667A; retrieved 2026-06-27. and applied mutation signature T508I/N667A to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 37°C, recombinant mutant T508I/N667A


column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'LP2', cellobiose phosphorolysis block: column 'kcat (s^-1)' = 2.61; column 'Km (mM)' = 2.9; column 'kcat/Km (M^-1 s^-1)' = 904.

normalized_value_unit_evidence: kcat: printed Table III cell 2.61 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 2.61 s^(-1). Km: printed Table III cell 2.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 2.9 mM. kcat/Km: printed Table III cell 904 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 904 / 1000 = 0.904 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row LP2 (T508A/N667T), cellobiose phosphorolysis block: kcat = 2.61 s^-1; Km = 2.9 mM; printed kcat/Km = 904 M^-1 s^-1.

row_label: Table III, row LP2 (T508A/N667T), cellobiose phosphorolysis columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature T508A/N667T; retrieved 2026-06-27. and applied mutation signature T508A/N667T to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 37°C, recombinant mutant T508A/N667T


column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'CP', cellobiose phosphorolysis block: column 'kcat (s^-1)' = 13.2; column 'Km (mM)' = 2.9; column 'kcat/Km (M^-1 s^-1)' = 4557.

normalized_value_unit_evidence: kcat: printed Table III cell 13.2 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 13.2 s^(-1). Km: printed Table III cell 2.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 2.9 mM. kcat/Km: printed Table III cell 4557 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4557 / 1000 = 4.557 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row CP (wild-type), cellobiose phosphorolysis block: kcat = 13.2 s^-1; Km = 2.9 mM; printed kcat/Km = 4557 M^-1 s^-1.

row_label: Table III, row CP (wild-type), cellobiose phosphorolysis columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature A397V/T508A/A512T/D557N/N667T/G681S; retrieved 2026-06-27. and applied mutation signature A397V/T508A/A512T/D557N/N667T/G681S to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 37°C, recombinant mutant A397V/T508A/A512T/D557N/N667T/G681S


sequence_source: UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature T508I/N667A; retrieved 2026-06-27.


proof_lines: pH 6.6, 37°C, recombinant wild-type enzyme


sequence_source: UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature A397V/T508A/A512T/D557N/N667T/G681S; retrieved 2026-06-27.


organism: Thermoclostridium stercorarium


organism: Thermosipho africanus

substrate_name: D-glucose

assay_conditions_summary: pH 7.5; 348.15 K; buffer a 200 microlitre reaction of 50 mM Tris-HCl

column_label: Table 3: Kinetic parameters for the synthetic reaction catalyzed by TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 3, row d-Glucose; column Km (mM) = 14.3; column kcat (s-1) = 30.3; column kcat/Km (s-1 mM-1) = 2.12. captured primary segment: d-Glucose | Km 14.3 mM | kcat 30.3 s-1 | kcat / Km 2.12 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 30.3 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 30.3 s^(-1); the exported value is 30.3 s^(-1). Km: printed Table 3 cell 14.3 mM; the column head prints mM, so no unit conversion applies and the paper value is 14.3 mM; the exported value is 14.3 mM. kcat/Km: printed Table 3 cell 2.12 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 2.12 s^(-1)*mM^(-1); the exported value 2.1188811188811187 s^(-1)*mM^(-1) is the full-precision quotient 30.3 / 14.3 = 2.1188811188811187 of the same two printed cells, and the printed efficiency cell 2.12 is that quotient written to the two decimals Table 3 uses.

raw_value_unit_evidence: Table 3, row d-Glucose: Km = 14.3 mM; kcat = 30.3 s-1; printed kcat/Km = 2.12 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 3, row d-Glucose

substrate: D-glucose


substrate_name: cellopentaose; D-xylose; cellotriose; D-glucose; cellotetraose; cellobiose; alpha-D-glucose 1-phosphate


substrate_name: cellopentaose

assay_conditions_summary: pH 7.5; 348.15 K; buffer a 40 microlitre reaction of 100 mM sodium phosphate

column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellopentaose; column Km (mM) = 0.060; column kcat (s-1) = 0.34; column kcat/Km (s-1 mM-1) = 5.67. captured primary segment: Cellopentaose | Km 0.060 mM | kcat 0.34 s-1 | kcat / Km 5.67 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.34 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.34 s^(-1); the exported value is 0.34 s^(-1). Km: printed Table 4 cell 0.060 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.06 mM; the exported value is 0.06 mM. kcat/Km: printed Table 4 cell 5.67 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 5.67 s^(-1)*mM^(-1); the exported value 5.666666666666667 s^(-1)*mM^(-1) is the full-precision quotient 0.34 / 0.060 = 5.666666666666667 of the same two printed cells, and the printed efficiency cell 5.67 is that quotient written to the two decimals Table 4 uses.

raw_value_unit_evidence: Table 4, row Cellopentaose: Km = 0.060 mM; kcat = 0.34 s-1; printed kcat/Km = 5.67 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellopentaose

substrate: cellopentaose


column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellobiose; column Km (mM) = 0.120; column kcat (s-1) = 0.23; column kcat/Km (s-1 mM-1) = 1.92. captured primary segment: Cellobiose | Km 0.120 mM | kcat 0.23 s-1 | kcat / Km 1.92 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.23 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.23 s^(-1); the exported value is 0.23 s^(-1). Km: printed Table 4 cell 0.120 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.12 mM; the exported value is 0.12 mM. kcat/Km: printed Table 4 cell 1.92 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 1.92 s^(-1)*mM^(-1); the exported value 1.9166666666666667 s^(-1)*mM^(-1) is the full-precision quotient 0.23 / 0.120 = 1.9166666666666667 of the same two printed cells, and the printed efficiency cell 1.92 is that quotient written to the two decimals Table 4 uses.

raw_value_unit_evidence: Table 4, row Cellobiose: Km = 0.120 mM; kcat = 0.23 s-1; printed kcat/Km = 1.92 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellobiose


substrate_name: D-Xylose

column_label: Table 3: Kinetic parameters for the synthetic reaction catalyzed by TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 3, row d-Xylose; column Km (mM) = 25.7; column kcat (s-1) = 1.37; column kcat/Km (s-1 mM-1) = 0.05. captured primary segment: d-Xylose | Km 25.7 mM | kcat 1.37 s-1 | kcat / Km 0.05 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.37 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 1.37 s^(-1); the exported value is 1.37 s^(-1). Km: printed Table 3 cell 25.7 mM; the column head prints mM, so no unit conversion applies and the paper value is 25.7 mM; the exported value is 25.7 mM. kcat/Km: printed Table 3 cell 0.05 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 0.05 s^(-1)*mM^(-1); the exported value 0.053307392996108954 s^(-1)*mM^(-1) is the full-precision quotient 1.37 / 25.7 = 0.053307392996108954 of the same two printed cells, and the printed efficiency cell 0.05 is that quotient written to the two decimals Table 3 uses.

raw_value_unit_evidence: Table 3, row d-Xylose: Km = 25.7 mM; kcat = 1.37 s-1; printed kcat/Km = 0.05 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 3, row d-Xylose

substrate: D-Xylose


substrate_name: cellotetraose

column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellotetraose; column Km (mM) = 0.062; column kcat (s-1) = 0.49; column kcat/Km (s-1 mM-1) = 7.91. captured primary segment: Cellotetraose | Km 0.062 mM | kcat 0.49 s-1 | kcat / Km 7.91 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.49 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.49 s^(-1); the exported value is 0.49 s^(-1). Km: printed Table 4 cell 0.062 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.062 mM; the exported value is 0.062 mM. kcat/Km: printed Table 4 cell 7.91 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 7.91 s^(-1)*mM^(-1); the exported value 7.903225806451613 s^(-1)*mM^(-1) is the quotient 0.49 / 0.062 = 7.903225806451613 of the two printed component cells, whereas the paper's own printed efficiency cell is 7.91; the printed cell governs and kcat_over_km is corrected to 7.91 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, row Cellotetraose: Km = 0.062 mM; kcat = 0.49 s-1; printed kcat/Km = 7.91 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellotetraose

substrate: cellotetraose


substrate_name: cellotriose

column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellotriose; column Km (mM) = 0.094; column kcat (s-1) = 0.28; column kcat/Km (s-1 mM-1) = 2.98. captured primary segment: Cellotriose | Km 0.094 mM | kcat 0.28 s-1 | kcat / Km 2.98 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.28 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.28 s^(-1); the exported value is 0.28 s^(-1). Km: printed Table 4 cell 0.094 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.094 mM; the exported value is 0.094 mM. kcat/Km: printed Table 4 cell 2.98 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 2.98 s^(-1)*mM^(-1); the exported value 2.9787234042553195 s^(-1)*mM^(-1) is the full-precision quotient 0.28 / 0.094 = 2.9787234042553195 of the same two printed cells, and the printed efficiency cell 2.98 is that quotient written to the two decimals Table 4 uses.

raw_value_unit_evidence: Table 4, row Cellotriose: Km = 0.094 mM; kcat = 0.28 s-1; printed kcat/Km = 2.98 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellotriose

substrate: cellotriose


substrate_name: alpha-D-glucose 1-phosphate

column_label: Table 3: Kinetic parameters for the synthetic reaction catalyzed by TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 3, row G-1-P; column Km (mM) = 1.57; column kcat (s-1) = 7.61; column kcat/Km (s-1 mM-1) = 4.85. captured primary segment: G-1-P | Km 1.57 mM | kcat 7.61 s-1 | kcat / Km 4.85 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 7.61 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 7.61 s^(-1); the exported value is 7.61 s^(-1). Km: printed Table 3 cell 1.57 mM; the column head prints mM, so no unit conversion applies and the paper value is 1.57 mM; the exported value is 1.57 mM. kcat/Km: printed Table 3 cell 4.85 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 4.85 s^(-1)*mM^(-1); the exported value 4.8471337579617835 s^(-1)*mM^(-1) is the full-precision quotient 7.61 / 1.57 = 4.8471337579617835 of the same two printed cells, and the printed efficiency cell 4.85 is that quotient written to the two decimals Table 3 uses.

raw_value_unit_evidence: Table 3, row G-1-P: Km = 1.57 mM; kcat = 7.61 s-1; printed kcat/Km = 4.85 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 3, row G-1-P

substrate: alpha-D-glucose 1-phosphate


organism: Thermotoga neapolitana


substrate_name: Phosphate; Cellobiose; Phosphate; Cellobiose; D-Glucose; D-Glucose 1-phosphate


substrate_name: Cellobiose

substrate: Cellobiose


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


organism: Cellulomonas gilvus

proof_lines: enzyme assay at 37°C in 50 mM Tris/HCl (pH 7.0)


substrate_name: methyl beta-D-glucoside

substrate: methyl beta-D-glucoside


proof_lines: pH 6.6, 30°C, recombinant His6-tagged enzyme

proof_lines: in presence of saturating concentrations of phosphate


organism: Ruminococcus albus


enzyme_display_name: FAD diphosphatase

substrate_name: FAD; H2O

sequence_source: UniProtKB reviewed entry P93740 / NUD23_ARATH, sequence version 2, accessed 2026-06-27

assay_conditions_summary: cofactor FAD

enzyme: FAD diphosphatase

substrate: FAD; H2O


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


organism: Chlamydomonas reinhardtii

substrate_name: FMN / FAD (30 degrees Celsius, pH 7.0)

assay_conditions_summary: pH 7; cofactor FAD

proof_lines: kcat is 0.103 sec(-1) with FMN as substrate (at 30 degrees Celsius and at pH 7.0) (PubMed:36273586). kcat is 0.395 sec(-1) with FAD as substrate (at 30 degrees Celsius and at pH 7.0) (PubMed:36273586).

substrate: FMN / FAD (30 degrees Celsius, pH 7.0)


organism: Homo sapiens

substrate_name: multiple FMN/FAD/ATP/NaPPi contexts

assay_conditions_summary: pH 7.5; cofactor FAD

proof_lines: kcat is 0.69 sec(-1) for FAD synthase activity using enzyme purified from E.coli (at 37 degrees Celsius and at pH 7.5) (PubMed:21951714). kcat is 0.69 sec(-1) for FAD synthase activity using enzyme purified from E.coli (at 37 degrees Celsiu

proof_lines: kcat is 0.042 sec(-1) for FAD synthase activity using C-terminal region (329-587) purified from E.coli (at 37 degrees Celsius and at pH 7.5) (PubMed:23443125). kcat is 0.0037 sec(-1) for the reverse pyrophosphorolytic reaction using C-termi

substrate: multiple FMN/FAD/ATP/NaPPi contexts


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: FAD with magnesium or cobalt ions (30 degrees Celsius, pH 7.0)

proof_lines: kcat is 0.2 sec(-1) with FAD as substrate in presence of magnesium ions (at 30 degrees Celsius and at pH 7.0) (PubMed:29902190). kcat is 0.38 sec(-1) with FAD as substrate in presence of cobalt ions (at 30 degrees Celsius and at pH 7.0) (Pu


substrate_name: FAD

substrate: FAD


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-glucosamine

substrate: D-glucosamine


organism: Saccharophagus degradans

substrate_name: cellobiose


organism: Thermotoga maritima

substrate_name: D-glucose


organism: unidentified


proof_lines: pH 7.0, temperature not specified in the publication


organism: Rattus norvegicus


enzyme_display_name: ferredoxin--NAD(+) reductase

organism: Bacillus subtilis

substrate_name: NADH; Oxidized ferredoxin

assay_conditions_summary: cofactor NADP+

enzyme: ferredoxin--NAD(+) reductase

substrate: NADH; Oxidized ferredoxin


organism: Acidaminococcus fermentans

substrate_name: oxidized [2Fe-2S] ferredoxin

proof_lines: at pH 6.8, temperature not specified in the publication

substrate: oxidized [2Fe-2S] ferredoxin


organism: Acinetobacter sp.

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: pH and temperature not specified in the publication

substrate: NADH


organism: Clostridium acetobutylicum

substrate_name: NAD+; Reduced ferredoxin; H+

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Reduced ferredoxin; H+


organism: Methylosinus trichosporium OB3b


organism: Mycobacterium sp.

substrate_name: oxidized ferredoxin

assay_conditions_summary: pH 8.6; cofactor NADH

substrate: oxidized ferredoxin


substrate_name: ferricytochrome c

proof_lines: recombinant ferredoxin with N-terminal His-tag, pH 8.6

proof_lines: recombinant ferredoxin with C-terminal His-tag, pH 8.6

substrate: ferricytochrome c


organism: Pseudomonas putida


organism: Pseudomonas sp.

assay_conditions_summary: cofactor NADPH


enzyme_display_name: feruloyl-CoA hydratase/lyase

organism: Pseudomonas fluorescens

substrate_name: feruloyl-CoA

sequence_source: source_record; direct UniProtKB O69762 check

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 3.72 sec(-1) with feruloyl-CoA as substrate.

enzyme: feruloyl-CoA hydratase/lyase

substrate: feruloyl-CoA


assay_conditions_summary: 303.15 K; cofactor CoA


sequence_source: direct UniProtKB O69762 exact accession lookup


sequence_variant_note: Resolved canonical sequence from direct UniProtKB O69762 exact accession lookup plus S123A one-based residue reconstruction and applied mutation signature S123A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct UniProtKB O69762 exact accession lookup plus Y239F one-based residue reconstruction and applied mutation signature Y239F to reconstruct the assayed variant sequence.


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


enzyme_display_name: allantoicase

substrate_name: allantoate

proof_lines: Vmax of the reaction with allantoate as substrate is nine times higher than that with ureidoglycolate.

enzyme: allantoicase

substrate: allantoate


organism: Burkholderia cepacia

substrate_name: (-)-Ureidoglycolate; H2O; Allantoate

sequence_source: UniProtKB Q39F96 direct accession lookup

substrate: (-)-Ureidoglycolate; H2O; Allantoate


organism: Chlamydomonas reinhardtii

substrate_name: Allantoate

sequence_source: UniProtKB P82678 direct accession lookup

substrate: Allantoate


substrate_name: H2O; Allantoate; Ureidoglycolate

sequence_source: UniProtKB P82678 direct lookup after parsing the source expression ((P82678)*3)*2 as a P82678 candidate

substrate: H2O; Allantoate; Ureidoglycolate


organism: Mus musculus

sequence_source: UniProtKB Q9JHX6 direct accession lookup


organism: Xenopus laevis

substrate_name: H2O; Allantoate

sequence_source: UniProtKB Q9W6S5 direct accession lookup

substrate: H2O; Allantoate


sequence_source: UniProtKB reviewed accession P82678 (ALLC_CHLRE); organism Chlamydomonas reinhardtii; EC 3.5.3.4; references PMID 10860551 and DOI 10.1006/abbi.2000.1833.


organism: Streptomyces viridiviolaceus


sequence_source: UniProtKB reviewed accession Q9W6S5 (ALLC_XENLA); organism Xenopus laevis; EC 3.5.3.4; references PMID 10864446 and DOI 10.1006/abbi.2000.1863.


enzyme_display_name: 13-deoxydaunorubicin hydroxylase

organism: Streptomyces sp. (strain C5)

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

proof_lines: kcat is 0.63 sec(-1) for oxidation on 13-dihydrodaunorubicin. kcat is 0.024 sec(-1) for hydroxylation on 13-deoxydaunorubicin. kcat is 0.00026 sec(-1) for oxidation on 13-dihydrocarminomycin. kcat is 0.00012 sec(-1) for hydroxylation on dau

enzyme: 13-deoxydaunorubicin hydroxylase


organism: Streptomyces sp.

sequence_source: UniProtKB reviewed accession Q59971 (DOXA_STRS5), sequence version 1; direct REST lookup 2026-06-27


substrate_name: daunorubicin

substrate: daunorubicin


organism: Aquifex aeolicus

sequence_source: UniProtKB accession O67625 direct lookup (UniProtKB reviewed (Swiss-Prot); Aquifex aeolicus (strain VF5); 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; EC 1.17.7.4; length 289)

proof_lines:
recombinant enzyme, pH 7.5, 60°C
Raw SKiD Env: Temp=60°C, pH=7.5


enzyme_display_name: chlorate reductase

organism: Azospira oryzae

substrate_name: bromate

sequence_source: UniProtKB accession G8QM55 direct lookup (UniProtKB unreviewed (TrEMBL); Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS); DMSO reductase family type II enzyme, molybdopterin subunit; EC not annotated; length 927)

enzyme: chlorate reductase

substrate: bromate


organism: Haloferax mediterranei

substrate_name: Chlorate

substrate: Chlorate


organism: Triticum aestivum

substrate_name: S-Adenosyl-L-methionine; Tricetin

sequence_source: UniProtKB accession Q38J50 direct lookup (UniProtKB reviewed (Swiss-Prot); Triticum aestivum; Tricetin 3',4',5'-O-trimethyltransferase; EC 2.1.1.169; length 356)

substrate: S-Adenosyl-L-methionine; Tricetin


sequence_source: UniProtKB accession Q84N28 direct lookup (UniProtKB reviewed (Swiss-Prot); Triticum aestivum; Flavone O-methyltransferase 1; EC 2.1.1.-; length 360)


substrate_name: tricetin

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

proof_lines: pH and temperature not specified in the publication, mutant W259A

substrate: tricetin


proof_lines: pH and temperature not specified in the publication, mutant E322I


proof_lines: pH and temperature not specified in the publication, mutant G305S


proof_lines: pH and temperature not specified in the publication, mutant D263N


proof_lines: pH and temperature not specified in the publication, mutant W259Y


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


enzyme_display_name: (R,S)-reticuline 7-O-methyltransferase

organism: Papaver somniferum

substrate_name: guaiacol

sequence_source: UniProtKB accession Q6WUC2 direct lookup (UniProtKB reviewed (Swiss-Prot); Papaver somniferum; (R,S)-reticuline 7-O-methyltransferase; EC 2.1.1.291; length 355)

proof_lines: pH 8.0, 35°C, cosubstrate guaiacol or (R)-reticuline

proof_lines: pH 8.0, 35°C, cosubstrate isovanillic acid

enzyme: (R,S)-reticuline 7-O-methyltransferase

substrate: guaiacol


substrate_name: (R)-reticuline

substrate: (R)-reticuline


substrate_name: (S)-reticuline

sequence_source: UniProtKB reviewed accession Q6WUC2

substrate: (S)-reticuline


enzyme_display_name: hydroxyethylthiazole kinase

organism: Staphylococcus aureus

sequence_source: UniProtKB reviewed accession Q6GEY3

enzyme: hydroxyethylthiazole kinase


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


enzyme_display_name: alkylglycerone-phosphate synthase

organism: Cavia porcellus

sequence_source: UniProtKB exact accession P97275 direct check on 2026-06-28

enzyme: alkylglycerone-phosphate synthase


organism: Trypanosoma brucei

substrate_name: Palmitoyldihydroxyacetone phosphate

sequence_source: UniProtKB exact accession O97157 direct check on 2026-06-28

substrate: Palmitoyldihydroxyacetone phosphate


enzyme_display_name: S-methyl-5-thioribose kinase

organism: Bacillus subtilis

substrate_name: ATP; 5-Methylthio-D-ribose

sequence_source: UniProtKB exact accession O31663 direct check on 2026-06-28

assay_conditions_summary: cofactor ATP

enzyme: S-methyl-5-thioribose kinase

substrate: ATP; 5-Methylthio-D-ribose


organism: Oryza sativa

sequence_source: UniProtKB exact accession Q7XR61 direct check on 2026-06-28


enzyme_display_name: inositol-1,3,4-trisphosphate 5/6-kinase

organism: Arabidopsis thaliana

sequence_source: UniProtKB exact accession O80568 direct check on 2026-06-28

enzyme: inositol-1,3,4-trisphosphate 5/6-kinase


organism: Bos taurus

sequence_source: UniProtKB exact accession P0C0T1 direct check on 2026-06-28


organism: Homo sapiens

sequence_source: UniProtKB exact accession Q13572 direct check on 2026-06-28


enzyme_display_name: pyruvate kinase

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB exact accession P14618 direct check on 2026-06-28

assay_conditions_summary: cofactor ADP

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Zea mays

substrate_name: ATP

substrate: ATP


enzyme_display_name: glucuronokinase

substrate_name: D-glucuronic acid

enzyme: glucuronokinase

substrate: D-glucuronic acid


enzyme_display_name: hydroxylysine kinase

substrate_name: (5R)-5-hydroxy-L-lysine (in the presence of 2 mM ATP)

enzyme: hydroxylysine kinase


organism: Unknown


organism: Aquifex aeolicus (strain VF5)


organism: Escherichia coli (strain K12)


organism: Stutzerimonas chloritidismutans

substrate_name: chlorate

sequence: LNMLEPVGETLASEYPYXK

wild_type_sequence: LNMLEPVGETLASEYPYXK

substrate: chlorate


substrate_name: palmitoyl-dihydroxyacetonephosphate (in the presence of 0.5 mM of hexadecanol)


organism: Rattus norvegicus

substrate_name: hexadecanol

substrate: hexadecanol


organism: Glycine max


organism: Plasmodium falciparum (isolate 3D7)

proof_lines: kcat is 1.3 sec(-1) for (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) (with methyl viologen as electron donor and at 30 degrees Celsius).


organism: Papaver somniferum

proof_lines: kcat is 0.1 sec(-1) with guaiacol as substrate. kcat is 0.07 sec(-1) with (S)-reticuline as substrate. kcat is 0.07 sec(-1) with (R)-reticuline as substrate. kcat is 0.03 sec(-1) with (R)-protosinomenine as substrate. kcat is 0.02 sec(-1) w


organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)

proof_lines: kcat is 15.4 sec(-1) with 5-deoxy-D-ribose as substrate. kcat is 6.2 sec(-1) with S-methyl-5-thio-D-ribose as substrate.


organism: Escherichia coli O45:K1 (strain S88 / ExPEC)

proof_lines: kcat is 10.6 sec(-1) with 5-methythioribose as substrate. kcat is 16.1 sec(-1) with 5-deoxyribose as substrate. kcat is 5.4 sec(-1) with S-ribosyl-L-homocysteine as substrate. kcat is 11.6 sec(-1) with ribose as substrate.


substrate_name: thiazole

proof_lines: kcat is 0.068 sec(-1) for thiazole. kcat is 0.069 sec(-1) for ATP.

substrate: thiazole


proof_lines: kcat is 1.79 sec(-1) for thiazole. kcat is 2.39 sec(-1) for ATP.


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: D-glycero-alpha-D-manno-heptose 1-phosphate (at pH 7.4 and 25 degrees Celsius)

proof_lines: kcat is 3.0 sec(-1) and 1.35 sec(-1) for D-glycero-alpha-D-manno-heptose 1-phosphate determined by 31P NMR and HPLC method, respectively.


organism: Aquifex aeolicus

substrate_name: Unknown

sequence_source: UniProtKB:O67625 (ISPH_AQUAE); reviewed canonical accession

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

substrate: Unknown


organism: Burkholderia glumae

assay_conditions_summary: pH 8

proof_lines: pH 8, temperature not specified in the publication


organism: Escherichia coli

sequence_source: UniProtKB:P62623 (ISPH_ECOLI); reviewed canonical accession


organism: Azospira oryzae

substrate_name: Chlorate


substrate_name: reduced benzyl viologen

assay_conditions_summary: cofactor FMN

substrate: reduced benzyl viologen


organism: Cavia porcellus


substrate_name: octadecanol

sequence_source: UniProtKB:Q9EQR2 (ADAS_RAT); reviewed canonical accession

substrate: octadecanol


organism: Bacillus subtilis

sequence_source: UniProtKB:O31663 (MTNK_BACSU); reviewed canonical accession

proof_lines:
37°C, approx. value
pH 8.0, 25°C


organism: Klebsiella aerogenes

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:Q9F0P1 (MTNK_KLEPN); reviewed canonical accession


organism: Lupinus luteus

assay_conditions_summary: pH 9.7; 308.15 K; cofactor ATP


organism: Bos taurus

sequence_source: UniProtKB:P0C0T1 (ITPK1_BOVIN); reviewed canonical accession


organism: Saccharomyces cerevisiae


organism: Saccharomyces pastorianus


organism: Schistosoma mansoni


organism: Spinacia oleracea


organism: Streptococcus mutans


organism: Streptococcus sanguis


organism: Synechococcus elongatus


organism: Toxoplasma gondii


organism: Trachemys scripta


organism: Trypanosoma brucei


organism: Trypanosoma cruzi


organism: Zapus hudsonius


organism: Danio rerio

substrate_name: D-glucuronate

assay_conditions_summary: pH 7.5; 308.15 K; cofactor ATP

substrate: D-glucuronate


organism: Lilium longiflorum

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Rattus norvegicus

substrate_name: GTP; 5-Hydroxy-L-lysine

substrate: GTP; 5-Hydroxy-L-lysine


enzyme_display_name: beta-lactamase

organism: Serratia fonticola

substrate_name: ceftazidime

proof_lines: at 25°C in 50 mM sodium phosphate (pH 7.0)

enzyme: beta-lactamase

substrate: ceftazidime


organism: Vigna radiata var. radiata

substrate_name: NADH

substrate: NADH


organism: Homo sapiens

proof_lines: pH 7.6, 37°C, in presence of CSN1, first order rate constant

proof_lines: pH 7.6, 37°C, in absence of CSN1, first order rate constant


proof_lines: pH 7.2, 37°C, versus 1D-myo-inositol-1,3,4-trisphosphate


organism: Bos taurus

substrate_name: Phosphoenolpyruvate; ADP


organism: Brassica napus


organism: Canis familiaris


organism: Columba livia


organism: Coprinopsis lagopus


organism: Cupriavidus necator


organism: Mus musculus


organism: Mustela vison


organism: Ricinus communis


organism: Unknown

substrate_name: H2O; Cephalothin

substrate: H2O; Cephalothin


organism: Escherichia coli

substrate_name: H2O; Nitrocefin

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: H2O; Nitrocefin


substrate_name: H2O; Cephaloridine

substrate: H2O; Cephaloridine


substrate_name: cefpirome

substrate: cefpirome


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: nitrocefin

substrate: nitrocefin


organism: Pseudomonas putida

substrate_name: H2O; Ampicillin

sequence_source: UniProtKB exact accession Q8GCU7 canonical sequence, direct lookup on 2026-06-28

substrate: H2O; Ampicillin


substrate_name: moxalactam

sequence_source: UniProtKB exact accession Q9RMI1 canonical sequence, direct lookup on 2026-06-28

substrate: moxalactam


organism: Shewanella livingstonensis

substrate_name: H2O; Amoxicillin

sequence_source: UniProtKB exact accession Q53BU1 canonical sequence, direct lookup on 2026-06-28

substrate: H2O; Amoxicillin


organism: Stenotrophomonas maltophilia

sequence_source: UniProtKB exact accession P52700 canonical sequence, direct lookup on 2026-06-28

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


organism: Klebsiella pneumoniae

substrate_name: ceftaxidime

sequence_source: UniProtKB:Q09HD0 direct accession lookup (release 2026_02)

substrate: ceftaxidime


substrate_name: temocillin

sequence_source: UniProtKB:Q6XEC0 direct accession lookup (release 2026_02)

substrate: temocillin


organism: Aeromonas sobria

substrate_name: H2O; Imipenem

substrate: H2O; Imipenem


organism: Enterobacter cloacae


organism: Haemophilus ducreyi


substrate_name: H2O; Benzylpenicillin

substrate: H2O; Benzylpenicillin


organism: Mycobacterium tuberculosis


organism: Proteus vulgaris


organism: Pseudomonas aeruginosa

substrate_name: Cefdinir; H2O

substrate: Cefdinir; H2O


substrate_name: ceftazidime

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


organism: Pseudomonas fluorescens

substrate_name: carbenicillin

substrate: carbenicillin


enzyme_display_name: deoxycytidine kinase

organism: Homo sapiens

substrate_name: cytidine

sequence_source: UniProtKB:P27707 direct REST lookup on 2026-06-28

enzyme: deoxycytidine kinase

substrate: cytidine


substrate_name: gemcitabine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature A100V/R104M/D133A to reconstruct the assayed variant sequence.

substrate: gemcitabine


substrate_name: Zalcitabine

substrate: Zalcitabine


substrate_name: Cytarabine

substrate: Cytarabine


substrate_name: ATP

mutation_signature: residues 65-79 deletion mutant with 2-deoxycytidine as cosubstrate

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

substrate: ATP


mutation_signature: residues 65-79 deletion mutant with 1-beta-D-arabinofuranosylcytosine as cosubstrate


mutation_signature: residues 65-79 deletion mutant with ATP as cosubstrate


proof_lines: less than 0.001 mM, residues 65-79 deletion mutant with UTP as cosubstrate


proof_lines: wild type enzyme with ATP as cosubstrate

proof_lines: wild type enzyme with UTP as cosubstrate

proof_lines: wild type enzyme with 1-beta-D-arabinofuranosylcytosine as cosubstrate


substrate_name: UTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature C185A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: C185A mutant enzyme with 2-deoxyadenosine as phosphate acceptor, pH 7.6

proof_lines: C185A mutant enzyme with 2-deoxycytidine as phosphate acceptor, pH 7.6

substrate: UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature C9S/C45S/C59S/C146S to reconstruct the assayed variant sequence.

proof_lines: cosubstrate L-2-deoxycytidine, mutant C9S/C45S/C59S/C146S, 37°C, pH 7.5

proof_lines: cosubstrate troxacitabine, mutant C9S/C45S/C59S/C146S, 37°C, pH 7.5

proof_lines: cosubstrate D-2-deoxycytidine, mutant C9S/C45S/C59S/C146S, 37°C, pH 7.5


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature S74D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature S74Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature S74A to reconstruct the assayed variant sequence.


substrate_name: Phosphoenolpyruvate; ADP

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

substrate: Phosphoenolpyruvate; ADP


organism: Saccharomyces cerevisiae


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


organism: Arabidopsis thaliana

substrate_name: ATP; D-Glucuronate

sequence_source: UniProtKB REST direct accession lookup Q93ZC9; checked 2026-06-28

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: allosteric interaction (Hill coefficient: 1.54)

substrate: ATP; D-Glucuronate


organism: Bacillus subtilis

substrate_name: GTP; 2'-Deoxycytidine

sequence_source: UniProtKB REST direct accession lookup P37529; checked 2026-06-28

substrate: GTP; 2'-Deoxycytidine


organism: Gallus gallus

substrate_name: deoxycytidine

sequence_source: UniProtKB REST direct accession lookup Q5ZMF3; checked 2026-06-28

proof_lines: at pH 8.0, temperature not specified in the publication

substrate: deoxycytidine


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
pH 7.6, 37°C, recombinant enzyme
cosubstrate ATP, 37°C, pH 7.6
pH 7.5, 37°C


organism: Unknown

substrate_name: deoxyguanosine

substrate: deoxyguanosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P27707 and applied mutation signature R104L/D133A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer of 100 mM Tris pH 7; cofactor NADH

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dG' under the R104L-D133A column group; column 'kcat (sec-1)' = 3.66; column 'Km (uM)' = 2266; column 'kcat/Km (x 10^-3)' = 1.6.

normalized_value_unit_evidence: Km: printed Table 4 cell 2266 in the column head unit micromolar; 2266 / 1000 = 2.266 mM, and the exported value is 2.266 mM. kcat: printed Table 4 cell 3.66 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 3.66 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 1.6 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 1.6 s^-1 mM^-1. The exported ratio carried on the same identity is 1.6151809355692852.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dG: kcat = 3.66 sec-1; Km = 2266 micromolar; printed kcat/Km = 1.6 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dG', R104L-D133A column group

table_label: Table 4: Comparison of catalytic efficiencies of new mutants with wild type dCK (Biochemistry 2009, 48(6):1256-1263)


sequence_source: UniProtKB:P27707 reviewed human DCK sequence, checked by UniProt REST on 2026-06-28

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'AraC' under the WT column group; column 'kcat (sec-1)' = 0.34; column 'Km (uM)' = 13.1; column 'kcat/Km (x 10^-3)' = 26.0.

normalized_value_unit_evidence: Km: printed Table 4 cell 13.1 in the column head unit micromolar; 13.1 / 1000 = 0.013099999999999999 mM, and the exported value is 0.0131 mM. kcat: printed Table 4 cell 0.34 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 0.34 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 26.0 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 26.0 s^-1 mM^-1. The exported ratio carried on the same identity is 25.954198473282442.

raw_value_unit_evidence: Table 4, WT column group, body row AraC: kcat = 0.34 sec-1; Km = 13.1 micromolar; printed kcat/Km = 26.0 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'AraC', WT column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'AraC' under the R104L-D133A column group; column 'kcat (sec-1)' = 0.79; column 'Km (uM)' = 50.6; column 'kcat/Km (x 10^-3)' = 15.6.

normalized_value_unit_evidence: Km: printed Table 4 cell 50.6 in the column head unit micromolar; 50.6 / 1000 = 0.0506 mM, and the exported value is 0.0506 mM. kcat: printed Table 4 cell 0.79 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 0.79 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 15.6 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 15.6 s^-1 mM^-1. The exported ratio carried on the same identity is 15.612648221343875.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row AraC: kcat = 0.79 sec-1; Km = 50.6 micromolar; printed kcat/Km = 15.6 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'AraC', R104L-D133A column group


substrate_name: L-thymidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 reviewed human DCK sequence, checked by UniProt REST on 2026-06-28; mutation_signature=R104M/D133A from selected batch record and applied mutation signature R104M/D133A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R104M/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

substrate: L-thymidine


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'Gem' under the R104L-D133A column group; column 'kcat (sec-1)' = 2.01; column 'Km (uM)' = 33.8; column 'kcat/Km (x 10^-3)' = 59.5.

normalized_value_unit_evidence: Km: printed Table 4 cell 33.8 in the column head unit micromolar; 33.8 / 1000 = 0.0338 mM, and the exported value is 0.0338 mM. kcat: printed Table 4 cell 2.01 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 2.01 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 59.5 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 59.5 s^-1 mM^-1. The exported ratio carried on the same identity is 59.467455621301774.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row Gem: kcat = 2.01 sec-1; Km = 33.8 micromolar; printed kcat/Km = 59.5 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'Gem', R104L-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'L-dT' under the R104L-D133A column group; column 'kcat (sec-1)' = 1.33; column 'Km (uM)' = 17.8; column 'kcat/Km (x 10^-3)' = 74.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 17.8 in the column head unit micromolar; 17.8 / 1000 = 0.0178 mM, and the exported value is 0.0178 mM. kcat: printed Table 4 cell 1.33 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.33 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 74.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 74.7 s^-1 mM^-1. The exported ratio carried on the same identity is 74.71910112359551.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row L-dT: kcat = 1.33 sec-1; Km = 17.8 micromolar; printed kcat/Km = 74.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'L-dT', R104L-D133A column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P27707 and applied mutation signature R104M/D133A to reconstruct the assayed variant sequence.

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'L-dT' under the R104M-D133A column group; column 'kcat (sec-1)' = 3.13; column 'Km (uM)' = 138.0; column 'kcat/Km (x 10^-3)' = 22.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 138.0 in the column head unit micromolar; 138.0 / 1000 = 0.138 mM, and the exported value is 0.138 mM. kcat: printed Table 4 cell 3.13 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 3.13 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 22.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 22.7 s^-1 mM^-1. The exported ratio carried on the same identity is 22.681159420289852.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row L-dT: kcat = 3.13 sec-1; Km = 138.0 micromolar; printed kcat/Km = 22.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'L-dT', R104M-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dA' under the R104L-D133A column group; column 'kcat (sec-1)' = 5.72; column 'Km (uM)' = 162.3; column 'kcat/Km (x 10^-3)' = 35.2.

normalized_value_unit_evidence: Km: printed Table 4 cell 162.3 in the column head unit micromolar; 162.3 / 1000 = 0.1623 mM, and the exported value is 0.1623 mM. kcat: printed Table 4 cell 5.72 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 5.72 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 35.2 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 35.2 s^-1 mM^-1. The exported ratio carried on the same identity is 35.243376463339494.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dA: kcat = 5.72 sec-1; Km = 162.3 micromolar; printed kcat/Km = 35.2 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dA', R104L-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'AraC' under the R104M-D133A column group; column 'kcat (sec-1)' = 1.43; column 'Km (uM)' = 136.5; column 'kcat/Km (x 10^-3)' = 10.5.

normalized_value_unit_evidence: Km: printed Table 4 cell 136.5 in the column head unit micromolar; 136.5 / 1000 = 0.1365 mM, and the exported value is 0.1365 mM. kcat: printed Table 4 cell 1.43 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.43 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 10.5 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 10.5 s^-1 mM^-1. The exported ratio carried on the same identity is 10.476190476190474.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row AraC: kcat = 1.43 sec-1; Km = 136.5 micromolar; printed kcat/Km = 10.5 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'AraC', R104M-D133A column group


substrate_name: D-thymidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 reviewed human DCK sequence, checked by UniProt REST on 2026-06-28; mutation_signature=R104L/D133A from selected batch record and applied mutation signature R104L/D133A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R104L/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

substrate: D-thymidine


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'Gem' under the R104M-D133A column group; column 'kcat (sec-1)' = 2.68; column 'Km (uM)' = 56.2; column 'kcat/Km (x 10^-3)' = 47.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 56.2 in the column head unit micromolar; 56.2 / 1000 = 0.0562 mM, and the exported value is 0.0562 mM. kcat: printed Table 4 cell 2.68 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 2.68 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 47.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 47.7 s^-1 mM^-1. The exported ratio carried on the same identity is 47.686832740213525.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row Gem: kcat = 2.68 sec-1; Km = 56.2 micromolar; printed kcat/Km = 47.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'Gem', R104M-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dT' under the R104M-D133A column group; column 'kcat (sec-1)' = 1.74; column 'Km (uM)' = 144.0; column 'kcat/Km (x 10^-3)' = 12.1.

normalized_value_unit_evidence: Km: printed Table 4 cell 144.0 in the column head unit micromolar; 144.0 / 1000 = 0.144 mM, and the exported value is 0.144 mM. kcat: printed Table 4 cell 1.74 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.74 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 12.1 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 12.1 s^-1 mM^-1. The exported ratio carried on the same identity is 12.083333333333334.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row D-dT: kcat = 1.74 sec-1; Km = 144.0 micromolar; printed kcat/Km = 12.1 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dT', R104M-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dC' under the R104L-D133A column group; column 'kcat (sec-1)' = 0.25; column 'Km (uM)' = 8.0; column 'kcat/Km (x 10^-3)' = 31.3.

normalized_value_unit_evidence: Km: printed Table 4 cell 8.0 in the column head unit micromolar; 8.0 / 1000 = 0.008 mM, and the exported value is 0.008 mM. kcat: printed Table 4 cell 0.25 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 0.25 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 31.3 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 31.3 s^-1 mM^-1. The exported ratio carried on the same identity is 31.25.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dC: kcat = 0.25 sec-1; Km = 8.0 micromolar; printed kcat/Km = 31.3 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dC', R104L-D133A column group


substrate_name: 2'-Deoxycytidine; ATP

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

substrate: 2'-Deoxycytidine; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature S74E to reconstruct the assayed variant sequence.


substrate_name: thymidine

sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133N to reconstruct the assayed variant sequence.

substrate: thymidine


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature A100V/R104M/D133S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104Q/D133N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104Q/D133G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P27707 direct lookup plus row-specific mutation reconstruction


sequence_source: UniProtKB P27707 direct lookup; canonical Homo sapiens deoxycytidine kinase sequence

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


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature A100V/R104M/D133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature D47E/R104Q/D133G/N163I/F242L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature A100V/R104M/D133T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P27707 and applied mutation signature R104L/D133A to reconstruct the assayed variant sequence.

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dT' under the R104L-D133A column group; column 'kcat (sec-1)' = 3.20; column 'Km (uM)' = 24.3; column 'kcat/Km (x 10^-3)' = 131.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 24.3 in the column head unit micromolar; 24.3 / 1000 = 0.024300000000000002 mM, and the exported value is 0.0243 mM. kcat: printed Table 4 cell 3.20 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 3.2 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 131.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 131.7 s^-1 mM^-1. The exported ratio carried on the same identity is 131.68724279835394.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dT: kcat = 3.20 sec-1; Km = 24.3 micromolar; printed kcat/Km = 131.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dT', R104L-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dC' under the R104M-D133A column group; column 'kcat (sec-1)' = 1.80; column 'Km (uM)' = 5.70; column 'kcat/Km (x 10^-3)' = 315.8.

normalized_value_unit_evidence: Km: printed Table 4 cell 5.70 in the column head unit micromolar; 5.70 / 1000 = 0.0057 mM, and the exported value is 0.0057 mM. kcat: printed Table 4 cell 1.80 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.8 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 315.8 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 315.8 s^-1 mM^-1. The exported ratio carried on the same identity is 315.7894736842105.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row D-dC: kcat = 1.80 sec-1; Km = 5.70 micromolar; printed kcat/Km = 315.8 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dC', R104M-D133A column group


enzyme_display_name: Beta-lactamase

organism: Acinetobacter baumannii

substrate_name: Imipenem

sequence_source: UniProtKB:Q5QT35 direct accession lookup (primary=Q5QT35)

enzyme: Beta-lactamase

substrate: Imipenem


substrate_name: Cefotaxime; H2O

sequence_source: UniProtKB:P05364 direct accession lookup (primary=P05364)

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: Cefotaxime; H2O


substrate_name: 7-aminocephalosporanic acid

sequence_source: UniProtKB:Q59401 direct accession lookup (primary=Q59401)

substrate: 7-aminocephalosporanic acid


organism: Bacillus subtilis (strain 168)

substrate_name: deoxyadenosine (with GTP at pH 8.5 and at 37 degrees Celsius)


substrate_name: deoxycytidine (dC)

substrate: deoxycytidine (dC)


organism: Mus musculus


organism: Bos taurus

substrate_name: cytosine arabinoside

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

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

substrate: cytosine arabinoside


substrate_name: troxacitabine

proof_lines: C9S/C45S/C59S/C146Smutant enzyme with UTP as phosphate donor, 37°C, pH 7.5

substrate: troxacitabine


proof_lines: C9S/C45S/C59S/C146S mutant enzyme with ATP as phosphate donor, 37°C, pH 7.5

proof_lines: C9S/C45S/C59S/C146S mutant enzyme with UTP as phosphate donor, 37°C, pH 7.5


proof_lines: pH 7.6, 37°C, enzyme mutant S74E, with co-substrate UTP

proof_lines: pH 7.6, 37°C, enzyme mutant S74E, with co-substrate ATP

proof_lines: pH 7.6, 37°C, enzyme mutant S74E, with substrates deoxycytidine and ATP, mixed inhibition


substrate_name: gemcitabine

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

proof_lines: pH 7.6, 37°C, wild-type enzyme, with co-substrate UTP

proof_lines: wild type enzyme with ATP as phosphate donor, 37°C, pH 7.5

substrate: gemcitabine


proof_lines:
cytosine arabinoside-induced cells
cosubstrate ATP, 37°C, pH 7.6
cosubstrate UTP, 37°C, pH 7.6


organism: Aeromonas hydrophila

substrate_name: benzylpenicillin

assay_conditions_summary: pH 6.5; 303.15 K; buffer 20 mM sodium cacodylate

proof_lines: mutant enzyme N116H/N220G, in 20 mM sodium cacodylate buffer, pH 6.5

substrate: benzylpenicillin


substrate_name: biapenem

proof_lines:
above, V67I mutant, 30°C, pH 6.5
V67I mutant, 30°C, pH 6.5

substrate: biapenem


proof_lines:
above, V67D mutant, 30°C, pH 6.5
V67D mutant, 30°C, pH 6.5


proof_lines:
T157A mutant, 30°C, pH 6.5
above, T157A mutant, 30°C, pH 6.5


substrate_name: nitrocefin

substrate: nitrocefin


proof_lines:
above, K224Q mutant, 30°C, pH 6.5
K224Q mutant, 30°C, pH 6.5


proof_lines:
above, H263A mutant, 30°C, pH 6.5
H263A mutant, 30°C, pH 6.5


proof_lines:
above, H196A mutant, 30°C, pH 6.5
H196A mutant, 30°C, pH 6.5


proof_lines:
H118A mutant, 30°C, pH 6.5
above, H118A mutant, 30°C, pH 6.5


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


organism: Aeromonas veronii

substrate_name: Unknown

sequence_source: UniProtKB:O31272 direct REST lookup 2026-06-28

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Aeromonas veronii bv. sobria


organism: Achromobacter sp. sallbros1

substrate_name: piperacillin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for E7BCS7

proof_lines:
pH 7.2, 25°C
or below, pH 7.2, 25°C

substrate: piperacillin


organism: Achromobacter xylosoxidans

substrate_name: cephalothin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for B3FIE3

proof_lines: Km above 2 mM, in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C

substrate: cephalothin


substrate_name: ampicillin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q5QT35

proof_lines:
37°C, pH 7.0
Raw SKiD Env: Temp=37°C, pH=7

substrate: ampicillin


substrate_name: ticarcillin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q5I2N2

substrate: ticarcillin


proof_lines: pH 7.2, temperature not specified in the publication, recombinant enzyme


substrate_name: Imipenem

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q9L4P2

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, without sodium bicarbonate, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, wild-type 0.85 enzyme