substrate_name: phosphate

column_label: Table 3 lists Apparent Km (mM) for phosphorolysis with Phosphate under the B. stearo(a) column as 1.1; the Kinetics prose also states Km for trehalose and Pi were 4.1 and 1.1 mM respectively.

raw_value_unit_evidence: Km raw_value=1.1 raw_unit=mM

row_label: Apparent Km (mM) / Phosphorolysis / Phosphate / B. stearo(a) column

substrate: phosphate


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

organism: Dictyostelium discoideum

substrate_name: GDP-L-fucose

source_db: brenda

verification_status: verified

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.

column_label: Abstract states apparent calculated Km values for GDP-Fuc and lacto-N-biose I are 1.27 microM and 2.80 mM, respectively.

raw_value_unit_evidence: Km raw_value=1.27 raw_unit=microM

row_label: Dictyostelium discoideum cytosolic fucosyltransferase with GDP-Fuc

table_label: PubMed abstract PMID 8849691

data_origin: experimental

substrate: GDP-L-fucose

status: verified

source: brenda


substrate_name: lacto-N-biose I

verification_status: unverified

enzyme: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate: lacto-N-biose I

status: unverified


organism: Rattus norvegicus

substrate_name: N-acetyllactosamine

source_db: uniprot

substrate: N-acetyllactosamine

source: uniprot


substrate_name: lacto-N-biose

substrate: lacto-N-biose


substrate_name: GDP-fucose

substrate: GDP-fucose


organism: Mus musculus

substrate_name: UDP-N-acetyl-D-galactosamine

proof_lines: pH 7.3, 37°C, membrane-bound complete enzyme

substrate: UDP-N-acetyl-D-galactosamine


organism: Escherichia coli

substrate_name: D-lactose

source_db: oed

kcat_over_km_origin: calculated

substrate: D-lactose

source: oed


substrate_name: GDP-beta-L-fucose

substrate: GDP-beta-L-fucose


enzyme_display_name: UDP-glucose flavonoid 3-O-glucosyltransferase 6

organism: Fragaria ananassa

proof_lines: The kinetic constants are determined for the recombinant GST-fusion protein.


substrate_name: UDP-glucose

enzyme: UDP-glucose flavonoid 3-O-glucosyltransferase 6

substrate: UDP-glucose


enzyme_display_name: UDP-glucose flavonoid 3-O-glucosyltransferase 7

substrate_name: isorhamnetin

substrate: isorhamnetin


enzyme: UDP-glucose flavonoid 3-O-glucosyltransferase 7


organism: Drosophila melanogaster

substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


organism: Solanum lycopersicum

substrate_name: p-coumaric acid

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

substrate: p-coumaric acid


substrate_name: ferulic acid

substrate: ferulic acid


substrate_name: caffeic acid

substrate: caffeic acid


substrate_name: Sinapic acid

substrate: Sinapic acid


substrate_name: UDPglucose

substrate: UDPglucose


organism: Lathyrus oleraceus


substrate_name: 1-naphthalene acetate

substrate: 1-naphthalene acetate


enzyme_display_name: 1,3-beta-D-glucan phosphorylase

organism: Unknown

substrate_name: laminaribiose

km_display: Not reported

enzyme: 1,3-beta-D-glucan phosphorylase

substrate: laminaribiose


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


substrate_name: Laminarihexaose

substrate: Laminarihexaose


substrate_name: laminaritriose

substrate: laminaritriose


substrate_name: laminaritetraose

substrate: laminaritetraose


substrate_name: Laminaripentaose

substrate: Laminaripentaose


substrate_name: Unknown

source_db: unknown

source_license: see source

substrate: Unknown

source: unknown


enzyme_display_name: UniProt P08037

organism: Bos taurus

substrate_name: UDP-galactose

source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt P08037

substrate: UDP-galactose

source: skid


enzyme_display_name: Beta-1,4-galactosyltransferase 1

substrate_name: D-GlcNAc

enzyme: Beta-1,4-galactosyltransferase 1

substrate: D-GlcNAc


organism: Streptococcus mutans

substrate_name: sucrose

substrate: sucrose


substrate_name: Sucrose; Dextran

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

substrate: Sucrose; Dextran


organism: Biomphalaria glabrata

substrate_name: UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) (at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7


enzyme_display_name: sinapate 1-glucosyltransferase

organism: Daucus carota subsp. sativus

substrate_name: sinapate

enzyme: sinapate 1-glucosyltransferase

substrate: sinapate


organism: Daucus carota


substrate_name: UDP-Gal

proof_lines: kcat is 3.14 min(-1) with UDP-Gal as substrate. kcat is 3.53 min(-1) with APDTRP glycopeptide as substrate. kcat is 1.91 min(-1) with APDSRP glycopeptide as substrate. kcat is 1.62 min(-1) with YAATGPF glycopeptide as substrate. kcat is 3.6

substrate: UDP-Gal


organism: Arabidopsis thaliana

substrate_name: UDPglucose; Sinapate

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

substrate: UDPglucose; Sinapate


substrate_name: Sinapate; UDPglucose

substrate: Sinapate; UDPglucose


substrate_name: UDPglucose; Indole-3-acetate

substrate: UDPglucose; Indole-3-acetate


substrate_name: UDPgalactose; GalNAc-alpha1-O-phenyl

substrate: UDPgalactose; GalNAc-alpha1-O-phenyl


substrate_name: Cinnamic acid; UDPglucose

substrate: Cinnamic acid; UDPglucose


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


substrate_name: UDPglucose; Ferulate

substrate: UDPglucose; Ferulate


organism: Punica granatum

proof_lines: kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is


proof_lines: kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is


enzyme_display_name: UDP-glycosyltransferase 75C1

enzyme: UDP-glycosyltransferase 75C1


organism: Zea mays

ki_unit: mM


substrate_name: APDTRP glycopeptide

substrate: APDTRP glycopeptide


enzyme_display_name: UDP-glycosyltransferase 84A2

enzyme: UDP-glycosyltransferase 84A2


enzyme_display_name: UDP-glycosyltransferase 84A1

enzyme: UDP-glycosyltransferase 84A1


substrate_name: ferulate

substrate: ferulate


substrate_name: caffeate

substrate: caffeate


substrate_name: cinnamate

substrate: cinnamate


enzyme_display_name: UDP-glycosyltransferase 84A3

enzyme: UDP-glycosyltransferase 84A3


substrate_name: abscisic acid

proof_lines:
SlUGT75C1
Solanum lycopersicum
abscisic acid

substrate: abscisic acid


substrate_name: UDP-glucose

column_label: Abstract reports KM values determined for IAA and UDP glucose as 0.8 and 0.7 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.7 mM raw_unit=mM

row_label: Maize IAA glucosyltransferase / UDP glucose

table_label: PubMed XML abstract PMID 33805949

substrate: UDP-glucose


raw_value_unit_evidence: Km raw_value=0.8 mM raw_unit=mM

row_label: Maize IAA glucosyltransferase / indole-3-acetic acid


column_label: Abstract reports the purified enzyme has an apparent Km for UDP-Gal of 630 microm using GalNAc-alpha1-O-phenyl as the acceptor.

raw_value_unit_evidence: Km raw_value=630 microm raw_unit=microM

row_label: Rat core 1 beta3-galactosyltransferase / UDP-Gal donor substrate

table_label: PubMed XML abstract PMID 11673471


enzyme_display_name: UDP-glycosyltransferase 75B1

column_label: Abstract reports apparent K(m) for pABA of 0.12 mm.

raw_value_unit_evidence: Km raw_value=0.12 mM raw_unit=mM

row_label: Arabidopsis UGT75B1 / pABA

table_label: PubMed XML abstract PMID 18385129

enzyme: UDP-glycosyltransferase 75B1


enzyme_display_name: UDP-glycosyltransferase 72E2

substrate_name: coniferyl aldehyde

column_label: Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2; row Coniferyl aldehyde; column 72E2 / K m (mM)

row_label: Coniferyl aldehyde

enzyme: UDP-glycosyltransferase 72E2

substrate: coniferyl aldehyde


substrate_name: sinapyl aldehyde

column_label: Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2; row Sinapyl aldehyde; column 72E2 / K m (mM)

row_label: Sinapyl aldehyde

substrate: sinapyl aldehyde


substrate_name: coniferyl alcohol

column_label: Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2; row Coniferyl alcohol; column 72E2 / K m (mM)

row_label: Coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: sinapyl alcohol

column_label: Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2; row Sinapyl alcohol; column 72E2 / K m (mM)

row_label: Sinapyl alcohol

substrate: sinapyl alcohol


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

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


organism: Homo sapiens


column_label: Figure 5 row Ferulic acid / UGT72E2; column K_M (mM) = 0.45.

row_label: Ferulic acid / UGT72E2

table_label: Figure 5, Characterization of the UGTs forming 4-O-glucosides with phenylpropanoids


substrate_name: sinapate

column_label: Figure 5 row Sinapic acid / UGT72E2; column K_M (mM) = 0.90.

normalized_value_unit_evidence: Km = 0.9 mM

row_label: Sinapic acid / UGT72E2

substrate: sinapate


enzyme_display_name: UDP-glycosyltransferase 72E3

column_label: Figure 5 row Sinapic acid / UGT72E3; column K_M (mM) = 0.18.

row_label: Sinapic acid / UGT72E3

enzyme: UDP-glycosyltransferase 72E3


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

column_label: Figure 5 row Sinapyl alcohol / UGT72E3; column K_M (mM) = 0.85.

row_label: Sinapyl alcohol / UGT72E3


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Spinacia oleracea

substrate_name: UDP-Gal

substrate: UDP-Gal


enzyme_display_name: UniProt Q9UBV7

substrate_name: UDP-alpha-D-galactose

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: UniProt Q9UBV7

substrate: UDP-alpha-D-galactose


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


substrate_name: UDP-xylose

substrate: UDP-xylose


enzyme_display_name: procollagen glucosyltransferase

organism: Rattus norvegicus

enzyme: procollagen glucosyltransferase


enzyme_display_name: Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3


substrate_name: ascorbate

enzyme: Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3

substrate: ascorbate


substrate_name: phenyl beta-D-galactoside

substrate: phenyl beta-D-galactoside


enzyme_display_name: Beta-1,4-galactosyltransferase 4

substrate_name: GlcNAc

enzyme: Beta-1,4-galactosyltransferase 4

substrate: GlcNAc


organism: Canis lupus familiaris

substrate_name: UDP-N-acetylgalactosamine

substrate: UDP-N-acetylgalactosamine


organism: Mus musculus

substrate_name: GD3(N-acetylneuraminic acid)

smiles: [Gd]

substrate: GD3(N-acetylneuraminic acid)


enzyme_display_name: UniProt O30511

organism: Helicobacter pylori

substrate_name: lactose

enzyme: UniProt O30511

substrate: lactose


substrate_name: N-acetyllactosamine

substrate: N-acetyllactosamine


substrate_name: lactosylceramide

substrate: lactosylceramide


substrate_name: gallic acid (at pH 5.0 and 30 degrees Celsius)

assay_conditions_summary: pH 5


substrate_name: 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: caffeic acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: cinnamic acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: coumaric acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: ferulic acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: sinapic acid (at pH 5.0 and 30 degrees Celsius)


substrate: gallic acid (at pH 5.0 and 30 degrees Celsius)


substrate: 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)


substrate: 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)


substrate: caffeic acid (at pH 5.0 and 30 degrees Celsius)


substrate: cinnamic acid (at pH 5.0 and 30 degrees Celsius)


substrate: coumaric acid (at pH 5.0 and 30 degrees Celsius)


substrate: ferulic acid (at pH 5.0 and 30 degrees Celsius)


substrate: sinapic acid (at pH 5.0 and 30 degrees Celsius)


proof_lines: at site Thr-9, hT2, single turnover event


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

mutation_type: substitution

proof_lines: at site Thr-9, hT2CD, at pre-steady state

proof_lines: at site Thr-9, hT2CD, single turnover event


proof_lines: at site Thr-3, hT2, single turnover event


proof_lines: at site Thr-13, hT2, at pre-steady state


proof_lines:
at site Thr-2 and Thr-12, hT10CD-hT2LD
at sites Thr-2 and Thr12, hT10CD-hT2LD


proof_lines:
at sites Thr-2 and Thr-12, hT10CD
at sites Thr-2 and Thr12, hT10CD


proof_lines:
at site Thr-2 and Thr-12, hT10
at sites Thr-2 and Thr12, hT10


substrate_name: UDP-N-acetyl-D-galactosamine

substrate: UDP-N-acetyl-D-galactosamine


substrate_name: STPSTPSTPSTPSTP

substrate: STPSTPSTPSTPSTP


substrate_name: UDP-galactose

proof_lines: 37°C, mutant enzyme R365K, hydrolase reaction

proof_lines: 37°C, mutant enzyme R365K, galactosyltransferase reaction

substrate: UDP-galactose


proof_lines: 37°C, mutant enzyme Q247E, hydrolase reaction

proof_lines: 37°C, mutant enzyme Q247E, galactosyltransferase reaction


proof_lines: 37°C, wild-type enzyme, hydrolase reaction

proof_lines: wild-type, N-acetyllactosamine, pH 6, 30°C

proof_lines: wild-type, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0


proof_lines: 37°C, mutant enzyme H280Q, galactosyltransferase reaction


proof_lines: 37°C, wild-type enzyme, galactosyltransferase reaction

proof_lines: wild-type kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0


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

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


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Withania somnifera

substrate_name: diosgenin

enzyme: sterol 3beta-glucosyltransferase

substrate: diosgenin


substrate_name: beta-sitosterol

proof_lines: activity is assayed radiometrically using UDP-[U-14C] glucose, at pH 8.0 and 37°C

substrate: beta-sitosterol


substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: stigmasterol

substrate: stigmasterol


substrate_name: 24-methylene cholesterol

substrate: 24-methylene cholesterol


enzyme_display_name: sucrose 6F-alpha-galactosyltransferase

organism: Sesamum indicum

substrate_name: UDPgalactose

enzyme: sucrose 6F-alpha-galactosyltransferase

substrate: UDPgalactose


substrate_name: sucrose

substrate: sucrose


substrate_name: ergosterol

substrate: ergosterol


substrate_name: brassicasterol

substrate: brassicasterol


substrate_name: solasodine

substrate: solasodine


organism: Cycas revoluta

substrate_name: methylazoxymethanol

substrate: methylazoxymethanol


substrate_name: UDPglucose

substrate: UDPglucose


substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


proof_lines: GalNac-T1 triple mutant D444A/D484A/D525A


mutation_type: deletion

proof_lines: inhibition of GalNAc-T1 mutant P-deltaN42


enzyme_display_name: isoflavone 7-O-glucosyltransferase

organism: Glycine max

substrate_name: daidzein

proof_lines: pH 8.5, 30°C, recombinant isozyme GmUGT3

proof_lines: pH 8.5, 30°C, recombinant isozyme GmUGT1

enzyme: isoflavone 7-O-glucosyltransferase

substrate: daidzein


proof_lines: purified enzyme, enzyme assay is run at pH 8.5 at 30°C


substrate_name: genistein

substrate: genistein


substrate_name: eriodictyol

column_label: Table 3 row Eriodictyol, column Km (uM), reports 18.0.

raw_value_unit_evidence: Eriodictyol row: Km 18.0 uM; Vmax 333.3 pkat/mg; Vmax/Km 18.5; Kcat/Km 2.66 uM^-1/s.

row_label: Eriodictyol

table_label: PDF Table 3, Substrate Specificities of the Purified AtGT-2 Recombinant Protein

substrate: eriodictyol


substrate_name: kaempferol

column_label: Table 3 row Kaempferol, column Km (uM), reports 26.3.

raw_value_unit_evidence: Kaempferol row: Km 26.3 uM; Vmax 333.3 pkat/mg; Vmax/Km 12.7; Kcat/Km 1.32 uM^-1/s.

row_label: Kaempferol

substrate: kaempferol


substrate_name: quercetin

column_label: Table 3 row Quercetin, column Km (uM), reports 35.3.

raw_value_unit_evidence: Quercetin row: Km 35.3 uM; Vmax 250.0 pkat/mg; Vmax/Km 7.1; Kcat/Km 0.41 uM^-1/s.

row_label: Quercetin

substrate: quercetin


organism: Sinapis alba

substrate_name: sitosterol

substrate: sitosterol


substrate_name: UDP-glucose

substrate: UDP-glucose


enzyme_display_name: xyloglucan 4-glucosyltransferase

enzyme: xyloglucan 4-glucosyltransferase


organism: Gardenia jasminoides


substrate_name: salicyl alcohol

substrate: salicyl alcohol


organism: Badhamia polycephala

substrate_name: poriferasterol

substrate: poriferasterol


organism: Solanum melongena


substrate_name: Genistein; UDPglucose

substrate: Genistein; UDPglucose


organism: Paris polyphylla var. yunnanensis


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E392A to reconstruct the assayed variant sequence.

proof_lines: E392A mutant, enzyme assay is run at pH 8.5 at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E456A to reconstruct the assayed variant sequence.

proof_lines: E456A mutant, enzyme assay is run at pH 8.5 at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E376A to reconstruct the assayed variant sequence.

proof_lines: E376A mutant, enzyme assay is run at pH 8.5 at 30°C


sequence_variant_note: Mutation signature E392D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: E392D mutant, enzyme assay is run at pH 8.5 at 30°C


enzyme_display_name: Isoflavone 7-O-glucosyltransferase 1

proof_lines: kcat is 0.74 sec(-1)for genistein (at pH 8.5 and 30 degrees Celsius).

enzyme: Isoflavone 7-O-glucosyltransferase 1


organism: Punica granatum

substrate_name: Unknown

proof_lines: kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is

substrate: Unknown


proof_lines: kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is


organism: Avena sativa


enzyme_display_name: UDP-glycosyltransferase 1

organism: Pueraria montana var. lobata

proof_lines: kcat is 1.1 sec(-1) with daidzein as substrate. kcat is 1.1 sec(-1) with genistein as substrate.

enzyme: UDP-glycosyltransferase 1


organism: Ogataea angusta

substrate_name: testosterone

verification_status: corrected

column_label: Table 2 row A7KAK6 T gives Km 837.9, kcat 351.9, and kcat/Km 0.42.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 351.9 s^-1; Km 0.8379 mM; kcat/Km 420 s^-1 mM^-1.

row_label: A7KAK6 / testosterone (T)

table_label: Table 2. Kinetic parameters of the UDPG-SGTases

substrate: testosterone

status: corrected


substrate_name: cholesterol

column_label: Table 2 row A7KAK6 C gives Km 67.2, kcat 650.6, and kcat/Km 9.7.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 650.6 s^-1; Km 0.0672 mM; kcat/Km 9700 s^-1 mM^-1.

row_label: A7KAK6 / cholesterol (C)

substrate: cholesterol


enzyme_display_name: Sterol 3-beta-glucosyltransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Sterol 3-beta-glucosyltransferase


enzyme_display_name: flavanone 7-O-beta-glucosyltransferase

organism: Lycium barbarum

substrate_name: naringenin

enzyme: flavanone 7-O-beta-glucosyltransferase

substrate: naringenin


organism: Arabidopsis thaliana

substrate_name: solasodine

substrate: solasodine


substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: brassicasterol

substrate: brassicasterol


substrate_name: ergosterol

substrate: ergosterol


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: stigmasterol

substrate: stigmasterol


substrate_name: beta-sitosterol

substrate: beta-sitosterol


substrate_name: gallic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / Gallic acid; column UGT84A23 Km (mM); cell 0.89 ± 0.07.

normalized_value_unit_evidence: Km normalized_value=0.89 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / Gallic acid: Km 0.89 ± 0.07 mM.

row_label: UGT84A23 / Gallic acid


substrate_name: 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / 4-HBA; column UGT84A23 Km (mM); cell 1.19 ± 0.03.

normalized_value_unit_evidence: Km normalized_value=1.19 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / 4-HBA: Km 1.19 ± 0.03 mM.

row_label: UGT84A23 / 4-HBA


substrate_name: 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / 3,4-DHBA; column UGT84A23 Km (mM); cell 2.46 ± 0.26.

normalized_value_unit_evidence: Km normalized_value=2.46 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / 3,4-DHBA: Km 2.46 ± 0.26 mM.


substrate_name: caffeic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / Caffeic acid; column UGT84A23 Km (mM); cell 1.06 ± 0.11.

normalized_value_unit_evidence: Km normalized_value=1.06 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / Caffeic acid: Km 1.06 ± 0.11 mM.

row_label: UGT84A23 / Caffeic acid


substrate_name: cinnamic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / Cinnamic acid; column UGT84A23 Km (mM); cell 1.12 ± 0.08.

normalized_value_unit_evidence: Km normalized_value=1.12 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / Cinnamic acid: Km 1.12 ± 0.08 mM.

row_label: UGT84A23 / Cinnamic acid


substrate_name: coumaric acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / Coumaric acid; column UGT84A23 Km (mM); cell 0.94 ± 0.13.

normalized_value_unit_evidence: Km normalized_value=0.94 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / Coumaric acid: Km 0.94 ± 0.13 mM.

row_label: UGT84A23 / Coumaric acid


substrate_name: ferulic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / Ferulic acid; column UGT84A23 Km (mM); cell 1.58 ± 0.01.

normalized_value_unit_evidence: Km normalized_value=1.58 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / Ferulic acid: Km 1.58 ± 0.01 mM.

row_label: UGT84A23 / Ferulic acid


substrate_name: sinapic acid (at pH 5.0 and 30 degrees Celsius)

column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A23 / Sinapic acid; column UGT84A23 Km (mM); cell 0.86 ± 0.05.

normalized_value_unit_evidence: Km normalized_value=0.86 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A23 / Sinapic acid: Km 0.86 ± 0.05 mM.

row_label: UGT84A23 / Sinapic acid


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / Gallic acid; column UGT84A24 Km (mM); cell 0.98 ± 0.01.

normalized_value_unit_evidence: Km normalized_value=0.98 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A24 / Gallic acid: Km 0.98 ± 0.01 mM.

row_label: UGT84A24 / Gallic acid

substrate: gallic acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / 4-HBA; column UGT84A24 Km (mM); cell 1.17 ± 0.03.

normalized_value_unit_evidence: Km normalized_value=1.17 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A24 / 4-HBA: Km 1.17 ± 0.03 mM.

row_label: UGT84A24 / 4-HBA

substrate: 4-hydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / 3,4-DHBA; column UGT84A24 Km (mM); cell 4.44 ± 0.73.

normalized_value_unit_evidence: Km normalized_value=4.44 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A24 / 3,4-DHBA: Km 4.44 ± 0.73 mM.

substrate: 3,4-dihydroxybenzoic acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / Caffeic acid; column UGT84A24 Km (mM); cell 1.77 ± 0.17.

normalized_value_unit_evidence: Km normalized_value=1.77 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A24 / Caffeic acid: Km 1.77 ± 0.17 mM.

row_label: UGT84A24 / Caffeic acid

substrate: caffeic acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / Cinnamic acid; column UGT84A24 Km (mM); cell 0.86 ± 0.09.

raw_value_unit_evidence: Table 1 row UGT84A24 / Cinnamic acid: Km 0.86 ± 0.09 mM.

row_label: UGT84A24 / Cinnamic acid

substrate: cinnamic acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / Coumaric acid; column UGT84A24 Km (mM); cell 1.06 ± 0.15.

raw_value_unit_evidence: Table 1 row UGT84A24 / Coumaric acid: Km 1.06 ± 0.15 mM.

row_label: UGT84A24 / Coumaric acid

substrate: coumaric acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / Ferulic acid; column UGT84A24 Km (mM); cell 1.32 ± 0.02.

normalized_value_unit_evidence: Km normalized_value=1.32 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A24 / Ferulic acid: Km 1.32 ± 0.02 mM.

row_label: UGT84A24 / Ferulic acid

substrate: ferulic acid (at pH 5.0 and 30 degrees Celsius)


column_label: Table 1. Kinetic parameters of pomegranate UGT84A23 and UGT84A24 towards selected phenolic acid substrates.; row UGT84A24 / Sinapic acid; column UGT84A24 Km (mM); cell 0.78 ± 0.02.

normalized_value_unit_evidence: Km normalized_value=0.78 normalized_unit=mM from Table 1 Km (mM); no unit conversion required.

raw_value_unit_evidence: Table 1 row UGT84A24 / Sinapic acid: Km 0.78 ± 0.02 mM.

row_label: UGT84A24 / Sinapic acid

substrate: sinapic acid (at pH 5.0 and 30 degrees Celsius)


substrate_name: Genistein

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D125A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

substrate: Genistein


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A6BM07 and applied mutation signature E376A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants), enzyme row E376A, Genistein column group; column kcat (s^-1) = 0.63; column Genistein Km (uM) = 4.5; column Genistein kcat/Km (s^-1 uM^-1) = 0.14. captured primary segment: Table 2 | Genistein | GmIF7GT E376A | kcat 0.63 s^-1 | Km 4.5 uM | kcat/Km 0.14 s^-1 uM^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.63 s^-1; the turnover column is printed per second, so no unit conversion applies and the value is 0.63 s^(-1). Km: printed Table 2 Genistein cell 4.5 uM; 1 uM is 1/1000 mM, so 4.5 / 1000 = 0.0045 mM. kcat/Km: printed Table 2 Genistein cell 0.14 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.14 x 1000 = 140.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row E376A, Genistein column group: kcat = 0.63 s^-1; Km = 4.5 uM; printed kcat/Km = 0.14 s^-1 uM^-1.

table_label: Table 2: Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants (J. Biol. Chem. 2007, 282(32):23581-23590); printed column heads Enzyme | kcat (s^-1) | Genistein Km (uM) | Genistein kcat/Km (s^-1 uM^-1) | UDP-glucose Km (uM) | UDP-glucose kcat/Km (s^-1 mM^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E392A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A6BM07 and applied mutation signature E392D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants), enzyme row E392D, Genistein column group; column kcat (s^-1) = 3.0; column Genistein Km (uM) = 0.77; column Genistein kcat/Km (s^-1 uM^-1) = 3.9. captured primary segment: Table 2 | Genistein | GmIF7GT E392D | kcat 3.0 s^-1 | Km 0.77 uM | kcat/Km 3.9 s^-1 uM^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.0 s^-1; the turnover column is printed per second, so no unit conversion applies and the value is 3.0 s^(-1). Km: printed Table 2 Genistein cell 0.77 uM; 1 uM is 1/1000 mM, so 0.77 / 1000 = 0.00077 mM. kcat/Km: printed Table 2 Genistein cell 3.9 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.9 x 1000 = 3900.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row E392D, Genistein column group: kcat = 3.0 s^-1; Km = 0.77 uM; printed kcat/Km = 3.9 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A6BM07 and applied mutation signature E456A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants), enzyme row E456A, Genistein column group; column kcat (s^-1) = 0.41; column Genistein Km (uM) = 2.6; column Genistein kcat/Km (s^-1 uM^-1) = 0.16. captured primary segment: Table 2 | Genistein | GmIF7GT E456A | kcat 0.41 s^-1 | Km 2.6 uM | kcat/Km 0.16 s^-1 uM^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.41 s^-1; the turnover column is printed per second, so no unit conversion applies and the value is 0.41 s^(-1). Km: printed Table 2 Genistein cell 2.6 uM; 1 uM is 1/1000 mM, so 2.6 / 1000 = 0.0026 mM. kcat/Km: printed Table 2 Genistein cell 0.16 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.16 x 1000 = 160.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row E456A, Genistein column group: kcat = 0.41 s^-1; Km = 2.6 uM; printed kcat/Km = 0.16 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H15A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A6BM07 and applied mutation signature H359A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants), enzyme row H359A, Genistein column group; column kcat (s^-1) = 0.59; column Genistein Km (uM) = 2.7; column Genistein kcat/Km (s^-1 uM^-1) = 0.22. captured primary segment: Table 2 | Genistein | GmIF7GT H359A | kcat 0.59 s^-1 | Km 2.7 uM | kcat/Km 0.22 s^-1 uM^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.59 s^-1; the turnover column is printed per second, so no unit conversion applies and the value is 0.59 s^(-1). Km: printed Table 2 Genistein cell 2.7 uM; 1 uM is 1/1000 mM, so 2.7 / 1000 = 0.0027 mM. kcat/Km: printed Table 2 Genistein cell 0.22 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.22 x 1000 = 220.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row H359A, Genistein column group: kcat = 0.59 s^-1; Km = 2.7 uM; printed kcat/Km = 0.22 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A6BM07 and applied mutation signature H368A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants), enzyme row H368A, Genistein column group; column kcat (s^-1) = 2.0; column Genistein Km (uM) = 4.9; column Genistein kcat/Km (s^-1 uM^-1) = 0.41. captured primary segment: Table 2 | Genistein | GmIF7GT H368A | kcat 2.0 s^-1 | Km 4.9 uM | kcat/Km 0.41 s^-1 uM^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.0 s^-1; the turnover column is printed per second, so no unit conversion applies and the value is 2.0 s^(-1). Km: printed Table 2 Genistein cell 4.9 uM; 1 uM is 1/1000 mM, so 4.9 / 1000 = 0.0049 mM. kcat/Km: printed Table 2 Genistein cell 0.41 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.41 x 1000 = 410.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row H368A, Genistein column group: kcat = 2.0 s^-1; Km = 4.9 uM; printed kcat/Km = 0.41 s^-1 uM^-1.


substrate_name: UDPglucose

substrate: UDPglucose


column_label: Table 2 row E376A, substrate UDP-glucose; raw cells kcat 0.63 +/- 0.01 s^-1, Km 2100 +/- 130 uM, kcat/Km 0.30 s^-1*mM^-1; normalized cells kcat 0.63 s^-1, Km 2.1 mM, kcat/Km 0.30 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.63 normalized_unit=s^-1; Km normalized_value=2.1 normalized_unit=mM; kcat/Km normalized_value=0.30 normalized_unit=s^-1*mM^-1; UDP-glucose catalytic efficiency printed in s^-1*mM^-1.

raw_value_unit_evidence: kcat raw_value=0.63 +/- 0.01 raw_unit=s^-1; Km raw_value=2100 +/- 130 raw_unit=uM; kcat/Km raw_value=0.30 raw_unit=s^-1*mM^-1

row_label: E376A / UDP-glucose

table_label: Table 2. Kinetic parameters for the enzyme from the roots of G. max seedlings, recombinant wild-type enzyme, and mutants


substrate_name: cholesterol

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

column_label: Table 2 row A7KAK6 C gives the exact cholesterol kinetic tuple.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 650.6 s^-1; Km 0.0672 mM; kcat/Km 9700 s^-1 mM^-1.

substrate: cholesterol


substrate_name: testosterone

column_label: Table 2 row A7KAK6 T gives the exact testosterone kinetic tuple.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 351.9 s^-1; Km 0.8379 mM; kcat/Km 420 s^-1 mM^-1.

row_label: A7KAK6 / testosterone (T)

substrate: testosterone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E392D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E456A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H359A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H368A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


organism: Kluyveromyces lactis

column_label: Table 2 row Q6CUV2 C gives Km 65.92, kcat 475.0, and kcat/Km 7.21.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 475.0 s^-1; Km 0.06592 mM; kcat/Km 7210 s^-1 mM^-1.

row_label: Q6CUV2 / cholesterol (C)


organism: Bos taurus

substrate_name: UDP-galactose

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

proof_lines: AGGL mutant, N-acetyllactosamine, pH 6, 30°C

proof_lines: mutant AGG, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0

substrate: UDP-galactose


substrate_name: UDP-N-acetylgalactosamine

substrate: UDP-N-acetylgalactosamine


substrate_name: N-acetyllactosamine

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

substrate: N-acetyllactosamine


proof_lines: AGGL mutant, UDP-N-acetylgalactosamine, pH 6, 30°C


substrate_name: lactose

proof_lines: mutant SGG kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0

substrate: lactose


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

organism: Homo sapiens

substrate_name: lacto-N-tetraose

proof_lines:
Se-gene encoded enzyme
H-gene encoded enzyme

substrate: lacto-N-tetraose


enzyme: type 1 galactoside alpha-(1,2)-fucosyltransferase


proof_lines:
H-gene encoded enzyme
Se-gene encoded enzyme


substrate_name: beta-D-galactose

substrate: beta-D-galactose


substrate_name: lacto-N-neotetraose

substrate: lacto-N-neotetraose


organism: Mus musculus

substrate_name: GDP-L-fucose

proof_lines: reaction with phenyl-beta-D-galactoside, recombinant enzyme

substrate: GDP-L-fucose


substrate_name: lactosylceramide

substrate: lactosylceramide


substrate_name: lacto-N-biose

substrate: lacto-N-biose


enzyme_display_name: UniProt E8MF13

organism: Bifidobacterium longum

substrate_name: lacto-N-biose I

enzyme: UniProt E8MF13

substrate: lacto-N-biose I


substrate_name: alpha-D-galactose 1-phosphate

substrate: alpha-D-galactose 1-phosphate


substrate_name: galacto-N-biose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P161S to reconstruct the assayed variant sequence.

substrate: galacto-N-biose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P161S/S336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V162T with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


enzyme_display_name: Hyaluronan synthase

organism: Pasteurella multocida

substrate_name: UDP-N-acetyl-D-glucosamine

enzyme: Hyaluronan synthase

substrate: UDP-N-acetyl-D-glucosamine


substrate_name: UDP-D-glucuronate

substrate: UDP-D-glucuronate


substrate_name: GDP-fucose

substrate: GDP-fucose


assay_conditions_summary: pH 6


substrate_name: phenyl beta-D-galactoside

substrate: phenyl beta-D-galactoside


organism: Rattus norvegicus

proof_lines:
enzyme FTB
pH 7.2, 37°C
enzyme FTA


proof_lines:
enzyme FTA
enzyme FTB


proof_lines:
pH 7.2, 37°C
enzyme FTA
enzyme FTB


substrate_name: phenyl beta-D-galactopyranoside

substrate: phenyl beta-D-galactopyranoside


organism: Glycine max

substrate_name: genistein

proof_lines: H15A mutant, enzyme assay is run at pH 8.5 at 30°C

substrate: genistein


proof_lines: H359A muant, enzyme assay is run at pH 8.5 at 30°C


proof_lines: D125A mutant, enzyme assay is run at pH 8.5 at 30°C


proof_lines: wild-type, enzyme assay is run at pH 8.5 at 30°C


proof_lines: H368A mutant, enzyme assay is run at pH 8.5 at 30°C


substrate_name: UDP-glucose

substrate: UDP-glucose


enzyme_display_name: UniProt B7SY86

organism: Rubrobacter xylanophilus

substrate_name: GDP-mannose

enzyme: UniProt B7SY86

substrate: GDP-mannose


enzyme_display_name: vomilenine glucosyltransferase

organism: Rauvolfia serpentina

substrate_name: Vomilenine

enzyme: vomilenine glucosyltransferase

substrate: Vomilenine


enzyme_display_name: UniProt A0A2R2JFJ4

organism: Persicaria tinctoria

enzyme: UniProt A0A2R2JFJ4


substrate_name: p-nitrophenyl-alpha-D-galactoside

substrate: p-nitrophenyl-alpha-D-galactoside


substrate_name: D-galactose

substrate: D-galactose


substrate_name: N-acetyllactosamine

substrate: N-acetyllactosamine


organism: Cicer arietinum

substrate_name: Biochanin A

substrate: Biochanin A


substrate_name: formononetin

substrate: formononetin


substrate_name: UDPglucose

substrate: UDPglucose


substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


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


enzyme_display_name: kojibiose phosphorylase

organism: Thermoanaerobacter brockii

substrate_name: beta-D-glucose 1-phosphate

enzyme: kojibiose phosphorylase

substrate: beta-D-glucose 1-phosphate


substrate_name: IgA hinge

proof_lines: +/-0.01 mM, mutant GalNAc-T2-D541A, pH7.4

proof_lines: +/-0.003 mM, mutant GalNAc-T2-D541A, pH7.4

proof_lines: +/-0.010 mM, mutant GalNAc-T2-D541A, pH7.4

substrate: IgA hinge


proof_lines: +/-0.001 mM, mutant GalNAc-T2-D541A, pH7.4


substrate_name: UDP-Gal

proof_lines: +/-0.005 mM, mutant GalNAc-T2-D541A, pH7.4

substrate: UDP-Gal


enzyme_display_name: cinnamate beta-D-glucosyltransferase

organism: Unknown

substrate_name: Unknown

enzyme: cinnamate beta-D-glucosyltransferase

substrate: Unknown


organism: Flammulina velutipes

substrate_name: alpha-D-glucose

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

substrate: alpha-D-glucose


substrate_name: phosphate

substrate: phosphate


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: alpha,alpha-trehalose

substrate: alpha,alpha-trehalose


organism: Lens culinaris

proof_lines:
with D-pinitol
with raffinose


substrate_name: raffinose

substrate: raffinose


substrate_name: D-pinitol

substrate: D-pinitol


organism: Sus scrofa


enzyme_display_name: alpha,alpha-trehalose synthase

organism: Pyrococcus horikoshii

substrate_name: ADP-alpha-D-glucose

enzyme: alpha,alpha-trehalose synthase

substrate: ADP-alpha-D-glucose


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


substrate_name: GDP-alpha-D-glucose

substrate: GDP-alpha-D-glucose


substrate_name: UDP

substrate: UDP


substrate_name: GDP

substrate: GDP


substrate_name: ADP

substrate: ADP


substrate_name: D-glucose

substrate: D-glucose


enzyme_display_name: sinapate 1-glucosyltransferase

organism: Brassica napus

substrate_name: Sinapic acid

enzyme: sinapate 1-glucosyltransferase

substrate: Sinapic acid


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: ferulate

substrate: ferulate


substrate_name: caffeate

substrate: caffeate


enzyme_display_name: N-acetyllactosamine synthase

organism: Bos taurus

substrate_name: UDP-galactose

enzyme: N-acetyllactosamine synthase

substrate: UDP-galactose


enzyme_display_name: UniProt A0A0H2URG7

organism: Streptococcus pneumoniae TIGR4

substrate_name: UDP-GlcNAc

enzyme: UniProt A0A0H2URG7

substrate: UDP-GlcNAc


enzyme_display_name: UniProt Q7KJA9

organism: Drosophila melanogaster

enzyme: UniProt Q7KJA9


substrate_name: UDPgalactose

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

substrate: UDPgalactose


substrate_name: N-acetylglucosamine

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

substrate: N-acetylglucosamine


substrate_name: GDP-L-fucose

substrate: GDP-L-fucose


proof_lines: in the absence of bovine serum albumin, at pH 7.0 and 30°C

proof_lines: in the presence of 12.5 mg/ml bovine serum albumin, at pH 7.0 and 30°C


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


enzyme_display_name: nigerose phosphorylase

organism: Lachnoclostridium phytofermentans

enzyme: nigerose phosphorylase


substrate_name: beta-D-glucopyranose 1-phosphate

substrate: beta-D-glucopyranose 1-phosphate


substrate_name: D-galactose

substrate: D-galactose


substrate_name: methyl alpha-D-glucopyranoside

substrate: methyl alpha-D-glucopyranoside


substrate_name: D-Xylose

substrate: D-Xylose


enzyme_display_name: UniProt Q5LH68

organism: Bacteroides fragilis

enzyme: UniProt Q5LH68


organism: Drosophila sp. (in: flies)

substrate_name: UDP-N-acetyl-D-galactosamine

substrate: UDP-N-acetyl-D-galactosamine


substrate_name: Unknown

substrate: Unknown


substrate_name: immunoglobulin G heavy chain

substrate: immunoglobulin G heavy chain


substrate_name: fetuin

substrate: fetuin


enzyme_display_name: cyanidin 3-O-galactosyltransferase

organism: Apium graveolens

substrate_name: cyanidin

enzyme: cyanidin 3-O-galactosyltransferase

substrate: cyanidin


organism: Daucus carota

substrate_name: pelargonidin

substrate: pelargonidin


substrate_name: peonidin

substrate: peonidin


substrate_name: UDP-alpha-D-galactose

proof_lines:
cosubstrate cyanidin, pH 8.6, 30°C
cosubstrate pelargonidin, pH 8.6, 30°C
cosubstrate peonidin, pH 8.6, 30°C

substrate: UDP-alpha-D-galactose


organism: Leishmania major

substrate_name: GDP-alpha-D-glucopyranose

substrate: GDP-alpha-D-glucopyranose


substrate_name: UDP-alpha-D-galactopyranose

substrate: UDP-alpha-D-galactopyranose


substrate_name: UDP-alpha-D-galactofuranose

substrate: UDP-alpha-D-galactofuranose


organism: Vitis vinifera

substrate_name: delphinidin 3-O-beta-D-glucoside

substrate: delphinidin 3-O-beta-D-glucoside


substrate_name: malvidin 3-O-beta-D-glucoside

substrate: malvidin 3-O-beta-D-glucoside


substrate_name: cyanidin 3-O-beta-D-glucoside

substrate: cyanidin 3-O-beta-D-glucoside


substrate_name: petunidin 3-O-beta-D-glucoside

substrate: petunidin 3-O-beta-D-glucoside


substrate_name: pelargonidin 3-O-beta-D-glucoside

substrate: pelargonidin 3-O-beta-D-glucoside


substrate_name: peonidin 3-O-beta-D-glucoside

substrate: peonidin 3-O-beta-D-glucoside


substrate_name: quercetin 3-O-beta-D-glucoside

substrate: quercetin 3-O-beta-D-glucoside


enzyme_display_name: UniProt Q21MB1

organism: Saccharophagus degradans

substrate_name: D-gluconate

enzyme: UniProt Q21MB1

substrate: D-gluconate


substrate_name: D-glucuronate

substrate: D-glucuronate


enzyme_display_name: UniProt Q9AFC7

organism: Amycolatopsis orientalis

substrate_name: desvancosaminyl-vancomycin

enzyme: UniProt Q9AFC7

substrate: desvancosaminyl-vancomycin


organism: Petunia x hybrida


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


substrate_name: UDP-alpha-D-glucopyranose

substrate: UDP-alpha-D-glucopyranose


substrate_name: GDP-alpha-D-mannopyranose

substrate: GDP-alpha-D-mannopyranose


enzyme_display_name: UniProt D6XZ22

organism: Salisediminibacterium selenitireducens

substrate_name: beta-D-glucose 1-phosphate

enzyme: UniProt D6XZ22

substrate: beta-D-glucose 1-phosphate


enzyme_display_name: 1,3-alpha-oligoglucan phosphorylase

enzyme: 1,3-alpha-oligoglucan phosphorylase


substrate_name: beta-D-glucopyranose 1-phosphate

substrate: beta-D-glucopyranose 1-phosphate


substrate_name: kojibiose

substrate: kojibiose


substrate_name: maltose

substrate: maltose


organism: Cyclamen purpurascens


organism: Trichormus variabilis (strain ATCC 29413 / PCC 7937)

substrate_name: UDP-Glc

substrate: UDP-Glc


organism: Streptomyces kanamyceticus

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

proof_lines: kcat is 3.36 min(-1) and 3.18 min(-1) for the reaction with paromamine as acceptor and UDP-alpha-D-kanosamine or UDP-alpha-D-glucose as donor, respectively.

source_databases_merged: brenda uniprot


substrate_name: UDP-alpha-D-kanosamine

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

substrate: UDP-alpha-D-kanosamine


substrate_name: paromamine

proof_lines: 37°C, pH not specified in the publication, cosubstrate: UDP-alpha-D-kanosamine

proof_lines: 37°C, pH not specified in the publication, cosubstrate: UDP-alpha-D-glucose

substrate: paromamine


enzyme_display_name: Trehalose-6-phosphate synthase

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

substrate_name: UDP-Glc (in the presence of polyanion)

enzyme: Trehalose-6-phosphate synthase

substrate: UDP-Glc (in the presence of polyanion)


enzyme_display_name: UniProt K7NBW3

organism: Siraitia grosvenorii

enzyme: UniProt K7NBW3


enzyme_display_name: mogroside IE synthase

substrate_name: mogrol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I to reconstruct the assayed variant sequence.

enzyme: mogroside IE synthase

substrate: mogrol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I/S15A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I/S15A/M76L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I/S15A/M76L/H47R to reconstruct the assayed variant sequence.


organism: Vitis amurensis

substrate_name: malvidin 3-O-beta-D-glucoside

substrate: malvidin 3-O-beta-D-glucoside


enzyme_display_name: beta-1,2-mannobiose phosphorylase

organism: Listeria innocua

substrate_name: D-fructose

proof_lines: kcat is 31 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 3.9 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 12 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kca

source_databases_merged: brenda skid uniprot

enzyme: beta-1,2-mannobiose phosphorylase

substrate: D-fructose


substrate_name: D-mannopyranose

substrate: D-mannopyranose


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


substrate_name: phosphate

proof_lines: 30°C, pH 7, cosubstrate: beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose

proof_lines: 30°C, pH 7, cosubstrate: beta-D-mannopyranosyl-(1->2)-D-mannopyranose

source_databases_merged: brenda skid

substrate: phosphate


enzyme_display_name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

organism: Dianthus caryophyllus

assay_conditions_summary: pH 5; 303.15 K; buffer 0.1 M citrate

column_label: Results prose page 3380, native Dc AA5GT clause of the kinetic parameter sentence: 'kcat for VG = 0.01 s^-1' and 'Km for VG = 46.5 uM'; the same clause also prints kcat for Cy3G = 0.06 s^-1 and Km for Cy3G = 13.0 uM, which belong to the acceptor axis; no kcat/Km is printed for native Dc AA5GT with VG.

normalized_value_unit_evidence: kcat: printed value 0.01 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.01 s^(-1). Km: printed value 46.5 uM; 46.5 / 1000 = 0.0465 mM. kcat/Km: no printed value for this pair, so the paper value 0.21505376344086022 s^(-1)*mM^(-1) is the quotient 0.01 / 0.0465 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Results prose, page 3380, native Dc AA5GT clause: kcat for VG = 0.01 s^-1; Km for VG = 46.5 uM; the article text prints no kcat/Km for native Dc AA5GT with VG.

row_label: page-3380 kinetic parameter sentence, native Dc AA5GT clause, VG donor values

table_label: Results prose, page 3380, section 'Kinetic Properties and Substrate Preferences of Acceptor and Donor Molecules of Dc AA5GT and Dg AA7GT' (The Plant Cell 2010, 22:3374-3389); the article has no kinetic table, the sentence cites the online-only Supplemental Table 3


substrate_name: cyanidin 3-O-beta-D-glucoside

proof_lines:
pH 5.0, 30°C, native enzyme
pH 5.0, 30°C, recombinant enzyme

enzyme: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

substrate: cyanidin 3-O-beta-D-glucoside


enzyme_display_name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

organism: Delphinium grandiflorum


enzyme: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)


enzyme_display_name: 1,2-beta-oligomannan phosphorylase

organism: Thermoanaerobacter sp.

substrate_name: alpha-D-mannose

assay_conditions_summary: pH 5; buffer pH 5

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Mannose; columns kcat s^-1 1.9; Km mM 0.41; printed kcat/Km 4.6; export-normalized kcat/Km 4.63414634146341

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.41 normalized_unit=mM; kcat/Km normalized_value=4.63414634146341 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=0.41 raw_unit=mM; printed kcat/Km=4.6 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Mannose

enzyme: 1,2-beta-oligomannan phosphorylase

substrate: alpha-D-mannose


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Fructose; columns kcat s^-1 2; Km mM 0.2; printed kcat/Km 10; export-normalized kcat/Km 10

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=2.0 raw_unit=s^-1; Km raw_value=0.20 raw_unit=mM; printed kcat/Km=10 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Fructose


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / donor a-Man1P; columns kcat s^-1 22; Km mM 1.4; printed kcat/Km 16; export-normalized kcat/Km 15.7142857142857

normalized_value_unit_evidence: kcat normalized_value=22 normalized_unit=s^-1; Km normalized_value=1.4 normalized_unit=mM; kcat/Km normalized_value=15.7142857142857 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=22 raw_unit=s^-1; Km raw_value=1.4 raw_unit=mM; printed kcat/Km=16 s^-1 mM^-1

row_label: Teth514_1788 / donor a-Man1P


proof_lines: cosubstrate: [(1->2)-beta-D-mannosyl]4, pH 5.0, 30°C, phosphorolytic reaction

proof_lines: cosubstrate: [(1->2)-beta-D-mannosyl]3, pH 5.0, 30°C, phosphorolytic reaction

proof_lines: cosubstrate: [(1->2)-beta-D-mannosyl]2, pH 5.0, 30°C, phosphorolytic reaction


enzyme_display_name: phlorizin synthase

organism: Malus domestica

substrate_name: phloretin

enzyme: phlorizin synthase

substrate: phloretin


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


enzyme_display_name: glucosylglycerate phosphorylase

organism: Xylanimonas protaetiae

substrate_name: D-glycerate

proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme H344A

enzyme: glucosylglycerate phosphorylase

substrate: D-glycerate


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342D


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme Q345A


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme P343A


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342A


substrate_name: L-Glycerate

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

proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme

substrate: L-Glycerate


substrate_name: sucrose

substrate: sucrose


substrate_name: fructose

substrate: fructose


enzyme_display_name: acylphloroglucinol glucosyltransferase

organism: Fragaria x ananassa

proof_lines:
pH 7.0, 30°C, allelic protein UGT71K3b
pH 7.0, 30°C, allelic protein UGT71K3a

enzyme: acylphloroglucinol glucosyltransferase


proof_lines:
pH 7.0, 30°C, allelic protein UGT71K3b
pH 7.0, 30°C, allelic protein UGT71K3a
pH 7.0, 30°C, UGT71K3a


enzyme_display_name: Beta-1,2-mannobiose phosphorylase

organism: Thermoanaerobacter sp. (strain X514)

substrate_name: D-mannose (for the synthetic reaction)

assay_conditions_summary: pH 5.5; buffer pH 5

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1789 / acceptor D-Mannose; columns Km mM 0.46

raw_value_unit_evidence: Km raw_value=0.46 raw_unit=mM for acceptor D-Mannose; paper row also reports kcat 10 s^-1 and kcat/Km 22 but the export row is Km-only.

row_label: Teth514_1789 / acceptor D-Mannose

enzyme: Beta-1,2-mannobiose phosphorylase

substrate: D-mannose (for the synthetic reaction)


substrate_name: D-fructose (for the synthetic reaction)

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1789 / acceptor D-Fructose; columns Km mM 0.69

raw_value_unit_evidence: Km raw_value=0.69 raw_unit=mM for acceptor D-Fructose; paper row also reports kcat 11 s^-1 and kcat/Km 16 but the export row is Km-only.

row_label: Teth514_1789 / acceptor D-Fructose

substrate: D-fructose (for the synthetic reaction)


substrate_name: alpha-D-mannose 1-phosphate (for the synthetic reaction)

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1789 / donor a-Man1P; columns Km mM 2.1

raw_value_unit_evidence: Km raw_value=2.1 raw_unit=mM for donor a-Man1P; paper row also reports kcat 12 s^-1 and kcat/Km 5.7 but the export row is Km-only.

row_label: Teth514_1789 / donor a-Man1P


organism: Allomeiothermus silvanus

proof_lines: kcat is 0.83 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)-D-glycerate for the phosphorolytic direction (at pH 6.0 and 42 degrees Celsius). kcat is 0.98 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.0 and 42 degrees Cel


enzyme_display_name: oleanolate 3-O-glucosyltransferase

organism: Barbarea vulgaris

substrate_name: glycyrrhetinic acid

enzyme: oleanolate 3-O-glucosyltransferase

substrate: glycyrrhetinic acid


enzyme_display_name: alpha-maltose-1-phosphate synthase

organism: Mycobacterium tuberculosis

substrate_name: ADP-alpha-D-glucose

assay_conditions_summary: pH 7; cofactor ADP

proof_lines: with 4.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C

proof_lines: with 2.5 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C

proof_lines: with 0.25 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C

enzyme: alpha-maltose-1-phosphate synthase

substrate: ADP-alpha-D-glucose


proof_lines: with 0.1 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C

proof_lines: with 4.0 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C

proof_lines: with 0.5 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C


organism: Leishmania major

substrate_name: UDP-alpha-D-glucopyranose

substrate: UDP-alpha-D-glucopyranose


substrate_name: UDP-alpha-D-galactopyranose

substrate: UDP-alpha-D-galactopyranose


substrate_name: UDP-alpha-D-galactofuranose

substrate: UDP-alpha-D-galactofuranose


substrate_name: GDP-alpha-D-mannopyranose

substrate: GDP-alpha-D-mannopyranose


substrate_name: GDP-alpha-D-glucopyranose

substrate: GDP-alpha-D-glucopyranose


organism: Bacteroides thetaiotaomicron


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


substrate_name: N,N'-diacetylchitobiose

substrate: N,N'-diacetylchitobiose


organism: Unknown

substrate_name: Unknown

assay_conditions_summary: pH 5.5; cofactor ADP

substrate: Unknown


smiles: C(C(C(C(C(C=O)O)O)O)O)OP(=O)(O)O

proof_lines:
37°C, pH 5.5, cosubstrate: UDP-glucose
37°C, pH 5.5, cosubstrate: ADP-glucose
37°C, pH 5.5, cosubstrate: TDP-glucose


enzyme_display_name: L-demethylnoviosyl transferase

organism: Streptomyces niveus

substrate_name: novobiocic acid

proof_lines: kcat is 313 min(-1) with novobiocic acid as substrate.

enzyme: L-demethylnoviosyl transferase

substrate: novobiocic acid


enzyme_display_name: Glucosylglycerate phosphorylase

organism: Escherichia coli (strain K12)

substrate_name: 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at pH 6.5 and 30 degrees Celsius)

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / alpha-(1,2)-D-glucose-D-glycerate; fixed substrate phosphate (20 mM); columns Km column raw 0.069 +/- 0.002 normalized 0.069 mM; export values for required/current metrics match these normalized values.

raw_value_unit_evidence: Km raw_value=0.069 +/- 0.002 raw_unit=mM

enzyme: Glucosylglycerate phosphorylase


substrate_name: phosphate (at pH 6.5 and 30 degrees Celsius)

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / phosphate; fixed substrate alpha-(1,2)-D-glucose-D-glycerate (1 mM); columns Km column raw 2.2 +/- 0.5 normalized 2.2 mM; export values for required/current metrics match these normalized values.

raw_value_unit_evidence: Km raw_value=2.2 +/- 0.5 raw_unit=mM


substrate_name: alpha-D-glucose 1-phosphate (at pH 6.5 and 30 degrees Celsius)

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / alpha-D-glucose-1-P; fixed substrate D-glycerate (4 mM); columns Km column raw 9.4 +/- 1.4 normalized 9.4 mM; export values for required/current metrics match these normalized values.

raw_value_unit_evidence: Km raw_value=9.4 +/- 1.4 raw_unit=mM


sequence_variant_note: Mutation signature T71K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
pH 7, 30°C, allelic protein UGT71K3b
pH 7, 30°C, allelic protein UGT71K3a


substrate_name: quercetin

proof_lines:
pH 7, 30°C, allelic protein UGT71K3a
pH 7, 30°C, allelic protein UGT71K3b

substrate: quercetin


substrate_name: pelargonidin

substrate: pelargonidin


substrate_name: kaempferol

substrate: kaempferol


substrate_name: acetylphloroglucinol

substrate: acetylphloroglucinol


organism: Escherichia coli

substrate_name: GDP-L-fucose

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

assay_conditions_summary: pH 8

proof_lines: kcat is 8.8 min(-1) with GDP-colitose as substrate. kcat is 12 min(-1) with GDP-L-fucose as substrate. kcat is 5.2 min(-1) with beta-Gal-(1->3)-GlcNAc as substrate.

substrate: GDP-L-fucose


enzyme_display_name: glucosylgalactose phosphorylase

organism: Paenibacillus polymyxa

enzyme: glucosylgalactose phosphorylase


substrate_name: phosphate

substrate: phosphate


substrate_name: D-galactopyranose

substrate: D-galactopyranose


substrate_name: alpha-D-glucopyranose 1-phosphate

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: L-arabinose

substrate: L-arabinose


enzyme_display_name: sterol 27-beta-glucosyltransferase

organism: Withania somnifera

enzyme: sterol 27-beta-glucosyltransferase


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: estradiol

substrate: estradiol


substrate_name: withanolide A

substrate: withanolide A


substrate_name: testosterone

substrate: testosterone


organism: Linum usitatissimum

substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


proof_lines: kcat is 1.9 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 2.0 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 25 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction).


enzyme_display_name: NDP-glycosyltransferase

organism: Bacillus subtilis

substrate_name: genistein

column_label: Table 1; row Genistein (4); columns Km, kcat, and kcat/Km; raw cells 22.6 +/- 3.1 uM, 1.6 +/- 0.1 s^-1, and 7.2 x 10^4 s^-1 M^-1.

row_label: Genistein (4)

table_label: Table 1: Kinetic parameters of Bs-YjiC towards apigenin (3) and genistein (4)

enzyme: NDP-glycosyltransferase

substrate: genistein


substrate_name: apigenin

column_label: Table 1; row Apigenin (3); columns Km, kcat, and kcat/Km; raw cells 19.4 +/- 2.6 uM, 1.9 +/- 0.1 s^-1, and 9.8 x 10^4 s^-1 M^-1.

row_label: Apigenin (3)

substrate: apigenin


enzyme_display_name: solabiose phosphorylase

organism: Paenibacillus borealis

substrate_name: D-galactose

proof_lines: kcat is 9.14 sec(-1) for the phosphorolysis of solabiose. kcat is 14.5 sec(-1) for the synthesis of solabiose.

enzyme: solabiose phosphorylase

substrate: D-galactose


substrate_name: solabiose

column_label: Prose reports phosphorolysis kcat and KmB where B is solabiose

row_label: Phosphorolysis of solabiose; B = solabiose

table_label: PMID 34997180 PMC8741936 section Enzymatic characteristics of PBOR_28850

substrate: solabiose


substrate_name: alpha-D-glucose 1-phosphate

column_label: Prose reports synthesis kcat and KmA where A is alpha-Glc1P

row_label: Synthesis of solabiose; A = alpha-Glc1P

substrate: alpha-D-glucose 1-phosphate


column_label: Prose reports phosphorolysis KmA 1.53 +/- 0.05 mM where A is inorganic phosphate

normalized_value_unit_evidence: 1.53 mM phosphate Km

row_label: Phosphorolysis of solabiose; A = inorganic phosphate


organism: Vigna angularis

proof_lines: enzyme hyperactivated with 3 mM benzalkonium chloride, at pH 7.0 and 30°C


organism: Limosilactobacillus fermentum

substrate_name: amylose

substrate: amylose


enzyme_display_name: Galactofuranosyltransferase GlfT2

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: UDP-Galf

proof_lines: kcat is 430 min(-1) for galtactose transfer on beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl.

enzyme: Galactofuranosyltransferase GlfT2

substrate: UDP-Galf


organism: Allomeiothermus silvanus (strain ATCC 700542 / DSM 9946 / NBRC 106475 / NCIMB 13440 / VI-R2)

substrate_name: alpha-D-glucose 1-phosphate (at pH 6.5 and 42 degrees Celsius)


substrate_name: D-glycerate (at pH 6.5 and 30 degrees Celsius)

proof_lines: kcat is 2.2 sec(-1) for phosphorolysis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate, kcat is 325 sec(-1) for glyceration of alpha-D-glucose 1-phosphate.


enzyme_display_name: Alpha-maltose-1-phosphate synthase

substrate_name: ADP-glucose (with 4 mM of G1P)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature G1P with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 97.9 sec(-1) for G1P as substrate (with 0.5 mM of ADP-glucose). kcat is 80.6 sec(-1) for G1P as substrate (with 4 mM of ADP-glucose). kcat is 39 sec(-1) for G1P as substrate (with 0.1 mM of ADP-glucose). kcat is 29.2 sec(-1) for ADP

enzyme: Alpha-maltose-1-phosphate synthase

substrate: ADP-glucose (with 4 mM of G1P)


substrate_name: G1P (with 4 mM of ADP-glucose)

substrate: G1P (with 4 mM of ADP-glucose)


enzyme_display_name: Galactofuranosyltransferase GlfT1

substrate_name: O-decenyl beta-D-Galf(1->6)-beta-D-Galf (at 37 degrees Celsius)

enzyme: Galactofuranosyltransferase GlfT1


organism: Perilla frutescens

substrate_name: UDPglucose; Cyanidin 3-O-glucoside

substrate: UDPglucose; Cyanidin 3-O-glucoside


organism: Streptomyces kanamyceticus

substrate_name: Paromamine; UDP-kanosamine

substrate: Paromamine; UDP-kanosamine


organism: Acholeplasma laidlawii

substrate_name: UDP-D-glucose; sn-1,2-Dioleoylglycerol

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

substrate: UDP-D-glucose; sn-1,2-Dioleoylglycerol


organism: Bifidobacterium adolescentis


substrate_name: Phosphate; Glucosylglycerate

substrate: Phosphate; Glucosylglycerate


enzyme_display_name: UniProt Q92DF6

organism: Listeria innocua

proof_lines: kcat is 31 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 3.9 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 12 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kca

enzyme: UniProt Q92DF6


organism: Thermoanaerobacter sp. (strain X514)

substrate_name: beta-1,2-Man2 (for the synthetic reaction)

proof_lines: kcat is 10 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 11 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 7.0 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kca


enzyme_display_name: 1,2-beta-oligomannan phosphorylase

organism: Thermoanaerobacter sp.

proof_lines: kcat is 1.9 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 2.0 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 25 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kc

enzyme: 1,2-beta-oligomannan phosphorylase


organism: Escherichia coli

substrate_name: GDP-colitose

substrate: GDP-colitose


substrate_name: alpha-glucan

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature G1P with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

substrate: alpha-glucan


enzyme_display_name: Protein O-glucosyltransferase 1

organism: Homo sapiens

substrate_name: Unknown

enzyme: Protein O-glucosyltransferase 1

substrate: Unknown


enzyme_display_name: NDP-glycosyltransferase YjiC

organism: Bacillus subtilis (strain 168)

substrate_name: 2-chloro-4-nitrophenyl glycoside

proof_lines: kcat is 1.9 sec(-1) with apigenin as substrate. kcat is 1.6 sec(-1) with genistein as substrate (PubMed:28315700). kcat is 164 min(-1) with 2-chloro-4-nitrophenyl glycoside as substrate (PubMed:33152360).

enzyme: NDP-glycosyltransferase YjiC

substrate: 2-chloro-4-nitrophenyl glycoside


enzyme_display_name: glucosylglycerate phosphorylase

organism: Meiothermus silvanus

substrate_name: Glucosylglycerate; Phosphate

enzyme: glucosylglycerate phosphorylase

substrate: Glucosylglycerate; Phosphate


organism: Spirochaeta thermophila


organism: Streptococcus mutans


organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)

substrate_name: poly(RboP)

substrate: poly(RboP)


enzyme_display_name: UDP-glycosyltransferase 71K3

organism: Fragaria ananassa

enzyme: UDP-glycosyltransferase 71K3


organism: Mycobacterium tuberculosis


organism: Gentiana triflora


enzyme_display_name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

organism: Dianthus caryophyllus

proof_lines: kcat is 0.06 sec(-1) with cyanidin 3-glucopyranoside (with native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.01 sec(-1) with 1-O-beta-D-vanillyl-glucose (with native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.07 sec(-1) wi


enzyme_display_name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

organism: Delphinium grandiflorum

proof_lines: kcat is 0.17 sec(-1) with cyanidin 3-glucopyranoside (at pH 5.0 and 30 degrees Celsius). kcat is 0.10 sec(-1) with 1-O-beta-D-vanillyl-glucose (at pH 5.0 and 30 degrees Celsius).


enzyme_display_name: L-noviosyl transferase

organism: Streptomyces niveus

substrate_name: Novobiocic acid; dTDP-L-noviose

enzyme: L-noviosyl transferase

substrate: Novobiocic acid; dTDP-L-noviose


organism: Acholeplasma laidlawii


enzyme: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)


substrate_name: Cyanidin 3,7-di-O-beta-D-glucoside

substrate: Cyanidin 3,7-di-O-beta-D-glucoside


substrate_name: Cyanidin 3-O-beta-D-glucoside

assay_conditions_summary: pH 6; 303.15 K; buffer 0.1 M citrate

column_label: Results prose page 3380, Dg AA7GT clause of the kinetic parameter sentence: 'kcat for Cy3G = 0.17 s^-1' and 'Km for Cy3G = 22.9 uM'; Results prose page 3381, recombinant AA7GT sentence: '7-O-glucosyltransferase activity for Cy3G (kcat/Km = 7.3 x 10^3)', in the s^-1 M^-1 unit the article states for kcat/Km on page 3380.

normalized_value_unit_evidence: kcat: printed value 0.17 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.17 s^(-1). Km: printed value 22.9 uM; 22.9 / 1000 = 0.0229 mM. kcat/Km: printed value 7.3 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7300 / 1000 = 7.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Results prose, page 3380, Dg AA7GT clause: kcat for Cy3G = 0.17 s^-1; Km for Cy3G = 22.9 uM. Results prose, page 3381, recombinant AA7GT sentence: printed kcat/Km for Cy3G = 7.3 x 10^3 s^-1 M^-1.

row_label: page-3380 kinetic parameter sentence, Dg AA7GT clause, Cy3G acceptor values; page-3381 recombinant AA7GT efficiency sentence, Cy3G value

table_label: Results prose, pages 3380 and 3381, section 'Kinetic Properties and Substrate Preferences of Acceptor and Donor Molecules of Dc AA5GT and Dg AA7GT' (The Plant Cell 2010, 22:3374-3389); the article has no kinetic table, the sentences cite the online-only Supplemental Table 3

substrate: Cyanidin 3-O-beta-D-glucoside


substrate_name: Cyanin

substrate: Cyanin


enzyme_display_name: beta-1,2-mannobiose phosphorylase

organism: Listeria innocua

column_label: Table 2; beta-1,2-Man2 row; kcat, KmA, kcat/KmA columns.

normalized_value_unit_evidence: Already in export units: kcat 35 s^-1; KmA 0.44 mM; kcat/KmA 79 s^-1 mM^-1. Export kcat/Km is 79.54545454545455, so not exact.

row_label: Table 2 beta-1,2-Man2 row

table_label: Tsuda et al. 2015, FEBS Letters, Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua; kinetic table evidence

enzyme: beta-1,2-mannobiose phosphorylase


column_label: Table 2; beta-1,2-Man3 row; kcat, KmA, kcat/KmA columns.

normalized_value_unit_evidence: Already in export units: kcat 12 s^-1; KmA 4.1 mM; kcat/KmA 3.0 s^-1 mM^-1. Export kcat/Km is 2.9268292682926833, so not exact.

row_label: Table 2 beta-1,2-Man3 row


substrate_name: alpha-D-mannose 1-phosphate

column_label: Table 1; alpha-Man1P donor row; kcat, Km, kcat/Km columns.

normalized_value_unit_evidence: Already in export units: kcat 33 s^-1; Km 3.1 mM; kcat/Km 11 s^-1 mM^-1. Export kcat/Km is 10.64516129032258, so not exact.

row_label: Table 1 alpha-Man1P donor row

substrate: alpha-D-mannose 1-phosphate


substrate_name: D-fructose

column_label: Table 1; d-Fructose acceptor row; kcat, Km, kcat/Km columns.

normalized_value_unit_evidence: Already in export units: kcat 3.9 s^-1; Km 1.5 mM; kcat/Km 2.7 s^-1 mM^-1. Export kcat/Km is 2.6, so not exact.

row_label: Table 1 d-Fructose acceptor row

substrate: D-fructose


substrate_name: D-mannopyranose

column_label: Table 1; d-Mannose acceptor row; kcat, Km, kcat/Km columns.

normalized_value_unit_evidence: Already in export units: kcat 31 s^-1; Km 2.1 mM; kcat/Km 15 s^-1 mM^-1. Export kcat/Km is 14.761904761904761, so not exact.

row_label: Table 1 d-Mannose acceptor row

substrate: D-mannopyranose


enzyme_display_name: phlorizin synthase

organism: Malus domestica

substrate_name: kaempferol

column_label: Table 4; row UDPG/Kaempferol - acceptor Kaempferol; Acceptors column Km (uM) raw value 2.09; Acceptors column kcat (s^-1) raw value 5.65; Acceptors column kcat/Km (s^-1*uM^-1) raw value 2.7

normalized_value_unit_evidence: kcat normalized_value=5.65 normalized_unit=s^-1; Km normalized_value=0.00209 normalized_unit=mM; kcat/Km normalized_value=2700 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5.65 raw_unit=s^-1; Km raw_value=2.09 raw_unit=uM; kcat/Km raw_value=2.7 raw_unit=s^-1*uM^-1

row_label: UDPG/Kaempferol - acceptor Kaempferol

table_label: Table 4. Kinetic parameters of Md P2GT for accepted donor and acceptor combinations

enzyme: phlorizin synthase

substrate: kaempferol


substrate_name: luteolin

column_label: Table 4; row UDPG/Luteolin - acceptor Luteolin; Acceptors column Km (uM) raw value 2.89; Acceptors column kcat (s^-1) raw value 3.24; Acceptors column kcat/Km (s^-1*uM^-1) raw value 1.12

normalized_value_unit_evidence: kcat normalized_value=3.24 normalized_unit=s^-1; Km normalized_value=0.00289 normalized_unit=mM; kcat/Km normalized_value=1120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.24 raw_unit=s^-1; Km raw_value=2.89 raw_unit=uM; kcat/Km raw_value=1.12 raw_unit=s^-1*uM^-1

row_label: UDPG/Luteolin - acceptor Luteolin

substrate: luteolin


substrate_name: isoliquiritigenin

column_label: Table 4; row UDPG/Isoliquiritigenin - acceptor Isoliquiritigenin; Acceptors column Km (uM) raw value 2.4; Acceptors column kcat (s^-1) raw value 4.35; Acceptors column kcat/Km (s^-1*uM^-1) raw value 1.81

normalized_value_unit_evidence: kcat normalized_value=4.35 normalized_unit=s^-1; Km normalized_value=0.0024 normalized_unit=mM; kcat/Km normalized_value=1810 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.35 raw_unit=s^-1; Km raw_value=2.4 raw_unit=uM; kcat/Km raw_value=1.81 raw_unit=s^-1*uM^-1

substrate: isoliquiritigenin


substrate_name: ADP-alpha-D-glucose

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

column_label: Table 4; row ADPG/Phloretin - donor ADPG; Donors column Km (uM) raw value 58.67; Donors column kcat (s^-1) raw value 4.65; Donors column kcat/Km (s^-1*uM^-1) raw value 0.08

normalized_value_unit_evidence: kcat normalized_value=4.65 normalized_unit=s^-1; Km normalized_value=0.05867 normalized_unit=mM; kcat/Km normalized_value=80 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.65 raw_unit=s^-1; Km raw_value=58.67 raw_unit=uM; kcat/Km raw_value=0.08 raw_unit=s^-1*uM^-1

row_label: ADPG/Phloretin - donor ADPG

substrate: ADP-alpha-D-glucose


substrate_name: phloretin

substrate: phloretin


substrate_name: quercetin

substrate: quercetin


substrate_name: UDP-alpha-D-galactose

column_label: Table 4; row UDP-Gal/Quercetin - donor UDP-Gal; Donors column Km (uM) raw value 26.19; Donors column kcat (s^-1) raw value 13.18; Donors column kcat/Km (s^-1*uM^-1) raw value 0.5

normalized_value_unit_evidence: kcat normalized_value=13.18 normalized_unit=s^-1; Km normalized_value=0.02619 normalized_unit=mM; kcat/Km normalized_value=500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=13.18 raw_unit=s^-1; Km raw_value=26.19 raw_unit=uM; kcat/Km raw_value=0.5 raw_unit=s^-1*uM^-1

row_label: UDP-Gal/Quercetin - donor UDP-Gal

substrate: UDP-alpha-D-galactose


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Thermoanaerobacter sp.

column_label: PDF Table 2. The kinetic parameters for the phosphorolytic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / b-1,2-Man2; columns kcat s^-1 1.9; Km mM 0.52; printed kcat/Km 3.7; export-normalized kcat/Km 3.65384615384615

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.52 normalized_unit=mM; kcat/Km normalized_value=3.65384615384615 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; KmA raw_value=0.52 raw_unit=mM; printed kcat/KmA=3.7 s^-1 mM^-1


column_label: PDF Table 2. The kinetic parameters for the phosphorolytic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / b-1,2-Man3; columns kcat s^-1 20; Km mM 0.92; printed kcat/Km 22; export-normalized kcat/Km 21.7391304347826

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=0.92 normalized_unit=mM; kcat/Km normalized_value=21.7391304347826 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=20 raw_unit=s^-1; KmA raw_value=0.92 raw_unit=mM; printed kcat/KmA=22 s^-1 mM^-1


substrate_name: alpha-D-mannose

assay_conditions_summary: pH 5; 303.15 K; buffer pH 5

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Mannose; columns kcat s^-1 1.9; Km mM 0.41; printed kcat/Km 4.6; export-normalized kcat/Km 4.63414634146341

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.41 normalized_unit=mM; kcat/Km normalized_value=4.63414634146341 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=0.41 raw_unit=mM; printed kcat/Km=4.6 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Mannose

substrate: alpha-D-mannose


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / donor a-Man1P; columns kcat s^-1 22; Km mM 1.4; printed kcat/Km 16; export-normalized kcat/Km 15.7142857142857

row_label: Teth514_1788 / donor a-Man1P


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Fructose; columns kcat s^-1 2; Km mM 0.2; printed kcat/Km 10; export-normalized kcat/Km 10

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=2.0 raw_unit=s^-1; Km raw_value=0.20 raw_unit=mM; printed kcat/Km=10 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Fructose


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


column_label: Table 1 row Phosphorolysis / Glucosylglycerate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: Phosphorolysis / Glucosylglycerate

table_label: Table 1. Apparent kinetic parameters of M. silvanus glucosylglycerate phosphorylase


substrate_name: alpha-D-glucopyranose 1-phosphate

column_label: Table 1 row Synthesis / alpha-D-Glucose 1-phosphate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: Synthesis / alpha-D-Glucose 1-phosphate

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: phosphate

smiles: O=P(O)(O)O

column_label: Table 1 row Phosphorolysis / Phosphate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km = 2.5 mM; kcat = 0.98 s^-1; paper kcat/Km = 0.40 s^-1*mM^-1; exported kcat_over_km = 0.392 s^-1*mM^-1

row_label: Phosphorolysis / Phosphate

substrate: phosphate


substrate_name: D-Glycerate

column_label: Table 1 row Synthesis / D-Glycerate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: Synthesis / D-Glycerate

substrate: D-Glycerate


substrate_name: phloroglucinol

substrate: phloroglucinol


substrate_name: pelargonidin

substrate: pelargonidin


enzyme_display_name: cyanidin 3-O-galactosyltransferase

organism: Camellia sinensis var. sinensis

substrate_name: cyanidin

column_label: Table 1 reports Cyanidin Km 32.64 +/- 3.48 uM, Vmax 3.29 +/- 0.21 uM min^-1, kcat 18.61 +/- 1.21 min^-1, kcat/Km 0.57 +/- 0.04 min^-1 uM^-1; Km matches, but converted kcat and kcat/Km differ slightly from current export

normalized_value_unit_evidence: Km normalized_value=0.03264 normalized_unit=mM; kcat normalized_value=0.3101666667 normalized_unit=s^-1; kcat_over_km normalized_value=9.5 normalized_unit=s^-1*mM^-1; current_export_kcat=0.31 s^-1; current_export_kcat_over_km=9.497549019607842 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=32.64 +/- 3.48 raw_unit=uM; kcat raw_value=18.61 +/- 1.21 raw_unit=min^-1; kcat_over_km raw_value=0.57 +/- 0.04 raw_unit=min^-1*uM^-1 for cyanidin

row_label: Table 1 Cyanidin row; Km, Vmax, kcat, and kcat/Km columns

table_label: PMID 34217130 ScienceDirect Table 1

enzyme: cyanidin 3-O-galactosyltransferase

substrate: cyanidin


substrate_name: myricetin

substrate: myricetin


substrate_name: delphinidin

column_label: Table 1 reports Delphinidin Km 45.59 +/- 3.12 uM, Vmax 6.63 +/- 0.1 uM min^-1, kcat 37.45 +/- 0.56 min^-1, kcat/Km 0.82 +/- 0.01 min^-1 uM^-1; Km matches, but converted kcat and kcat/Km differ slightly from current export

normalized_value_unit_evidence: Km normalized_value=0.04559 normalized_unit=mM; kcat normalized_value=0.6241666667 normalized_unit=s^-1; kcat_over_km normalized_value=13.6666666667 normalized_unit=s^-1*mM^-1; current_export_kcat=0.624 s^-1; current_export_kcat_over_km=13.687212107918404 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=45.59 +/- 3.12 raw_unit=uM; kcat raw_value=37.45 +/- 0.56 raw_unit=min^-1; kcat_over_km raw_value=0.82 +/- 0.01 raw_unit=min^-1*uM^-1 for delphinidin

row_label: Table 1 Delphinidin row; Km, Vmax, kcat, and kcat/Km columns

substrate: delphinidin


enzyme_display_name: UniProt P00491

organism: Homo sapiens

substrate_name: Methylthioinosine

enzyme: UniProt P00491

substrate: Methylthioinosine


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


enzyme_display_name: UniProt P0ABP8

organism: Escherichia coli

enzyme: UniProt P0ABP8


enzyme_display_name: UniProt P55859

organism: Bos taurus

substrate_name: Inosine

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

enzyme: UniProt P55859

substrate: Inosine


enzyme_display_name: UniProt Q2HXR2

organism: Toxoplasma gondii

substrate_name: guanosine

enzyme: UniProt Q2HXR2

substrate: guanosine


substrate_name: deoxyinosine

substrate: deoxyinosine


enzyme_display_name: UniProt Q6CSZ6

organism: Kluyveromyces lactis

substrate_name: Xanthosine

enzyme: UniProt Q6CSZ6

substrate: Xanthosine


substrate_name: adenosine

substrate: adenosine


substrate_name: nicotinamide riboside

substrate: nicotinamide riboside


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


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=5.7


substrate_name: deoxyguanosine

substrate: deoxyguanosine


proof_lines:
Raw SKiD Env: Temp=-----, pH=5.7
Raw SKiD Env: Temp=-----, pH=6.5


substrate_name: xanthine

proof_lines:
Raw SKiD Env: Temp=-----, pH=6
Raw SKiD Env: Temp=-----, pH=7.5

substrate: xanthine


substrate_name: guanine

substrate: guanine


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: UniProt P56463

organism: Helicobacter pylori

enzyme: UniProt P56463


enzyme_display_name: UniProt P45563

enzyme: UniProt P45563


substrate_name: cyanidin 3-O-beta-D-glucoside

column_label: Primary prose labels cyanidin 3-glucoside Km 20.9 uM.

raw_value_unit_evidence: cyanidin 3-glucoside Km 20.9 uM

row_label: cyanidin 3-glucoside

table_label: Recombinant Gt5GT7 substrate-specificity prose

substrate: cyanidin 3-O-beta-D-glucoside


substrate_name: delphinidin 3-O-beta-D-glucoside

column_label: Primary prose labels delphinidin 3-glucoside Km 29.5 uM.

raw_value_unit_evidence: delphinidin 3-glucoside Km 29.5 uM

row_label: delphinidin 3-glucoside

substrate: delphinidin 3-O-beta-D-glucoside


substrate_name: pelargonidin 3-glucoside

column_label: Primary prose labels pelargonidin 3-glucoside Km 12.2 mM.

normalized_value_unit_evidence: Km 12.2 mM

raw_value_unit_evidence: pelargonidin 3-glucoside Km 12.2 mM

row_label: pelargonidin 3-glucoside

substrate: pelargonidin 3-glucoside


substrate_name: malvidin 3-glucoside

column_label: Primary prose labels malvidin 3-glucoside Km 3.4 mM.

normalized_value_unit_evidence: Km 3.4 mM

raw_value_unit_evidence: malvidin 3-glucoside Km 3.4 mM

row_label: malvidin 3-glucoside

substrate: malvidin 3-glucoside


column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / alpha-(1,2)-D-glucose-D-glycerate; fixed substrate phosphate (20 mM); columns kcat column raw 2.1 +/- 0.2 normalized 2.1 s^-1; Km column raw 0.069 +/- 0.002 normalized 0.069 mM; kcat/Km column raw (3.1 +/- 0.1) x 10^4 M^-1 s^-1 normalized from same-row kcat and Km as 30.434782608695652 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=2.1 normalized_unit=s^-1; Km normalized_value=0.069 normalized_unit=mM; kcat/Km normalized_value=30.434782608695652 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=(3.1 +/- 0.1) x 10^4 M^-1 s^-1


enzyme_display_name: Phloretin 2'-O-glucosyltransferase

substrate_name: phloretin

enzyme: Phloretin 2'-O-glucosyltransferase

substrate: phloretin


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: GDP-beta-L-colitose

substrate: GDP-beta-L-colitose


enzyme: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)


substrate_name: Cyanidin 3,7-di-O-beta-D-glucoside

substrate: Cyanidin 3,7-di-O-beta-D-glucoside


substrate_name: Cyanidin 3-O-beta-D-glucoside

column_label: Publisher PDF page 7 kinetic prose for kcat and Km; page 8 prose for explicit kcat/Km; page 9 Table 2 confirms Cyanidin 3-glucoside is the active acceptor.

normalized_value_unit_evidence: kcat=0.07 s^-1; Km=0.0065 mM; explicit efficiency=10.0 s^-1 mM^-1.

raw_value_unit_evidence: kcat(Cy3G)=0.07 s^-1; Km(Cy3G)=6.5 microM; later main prose gives kcat/Km(Cy3G)=1.0 x 10^4 s^-1 M^-1.

row_label: Recombinant Dc AA5GT with Cy3G

table_label: Main-text kinetic prose citing Supplemental Table 3; explicit main-text efficiency comparison

substrate: Cyanidin 3-O-beta-D-glucoside


substrate_name: Cyanin

substrate: Cyanin


enzyme_display_name: NDP-glycosyltransferase

organism: Bacillus subtilis

substrate_name: apigenin

column_label: Table 1; row Apigenin (3); columns Km, kcat, and kcat/Km; raw cells 19.4 +/- 2.6 uM, 1.9 +/- 0.1 s^-1, and 9.8 x 10^4 s^-1 M^-1.

row_label: Apigenin (3)

enzyme: NDP-glycosyltransferase

substrate: apigenin


substrate_name: genistein

column_label: Table 1; row Genistein (4); columns Km, kcat, and kcat/Km; raw cells 22.6 +/- 3.1 uM, 1.6 +/- 0.1 s^-1, and 7.2 x 10^4 s^-1 M^-1.

row_label: Genistein (4)

substrate: genistein


enzyme_display_name: glucosylglycerate phosphorylase

organism: Winmispira thermophila

substrate_name: D-glycerate

enzyme: glucosylglycerate phosphorylase

substrate: D-glycerate


substrate_name: alpha-D-glucopyranose 1-phosphate

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: UDP-Glc

substrate: UDP-Glc


enzyme_display_name: Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase 1

organism: Perilla frutescens


organism: Vitis amurensis

substrate_name: malvidin 3-O-beta-D-glucoside

substrate: malvidin 3-O-beta-D-glucoside


substrate_name: UDP-Glc (in the presence of DOPG at 31%)


enzyme_display_name: L-demethylnoviosyl transferase

organism: Streptomyces niveus

substrate_name: novobiocic acid

enzyme: L-demethylnoviosyl transferase

substrate: novobiocic acid


enzyme_display_name: Protein O-glucosyltransferase 1

enzyme: Protein O-glucosyltransferase 1


organism: Campylobacter jejuni

proof_lines: recombinant mutant K75A/R72A/K68A, pH 7.5, 25°C


proof_lines: recombinant mutant K75A/R72A, pH 7.5, 25°C


proof_lines: recombinant mutant R72A/K68A, pH 7.5, 25°C


proof_lines: recombinant wild-type enzyme, pH 7.5, 25°C


substrate_name: phosphate

substrate: phosphate


organism: Mycobacterium tuberculosis

substrate_name: UDP-alpha-D-galactofuranose

proof_lines: mutant enzyme H413S, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C

substrate: UDP-alpha-D-galactofuranose


proof_lines: mutant enzyme E300S, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C


proof_lines: mutant enzyme W399S, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C


proof_lines: wild type enzyme, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C


enzyme_display_name: UniProt A0A0H3JPC6

organism: Staphylococcus aureus

substrate_name: UDP-N-acetyl-D-glucosamine

enzyme: UniProt A0A0H3JPC6

substrate: UDP-N-acetyl-D-glucosamine


organism: Drosophila melanogaster

substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


substrate_name: EA2 peptide

substrate: EA2 peptide


substrate_name: lacto-N-fucopentaose I

substrate: lacto-N-fucopentaose I


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

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


enzyme_display_name: N-acetyllactosamine synthase

substrate_name: asialo-agalacto-transferrin

enzyme: N-acetyllactosamine synthase

substrate: asialo-agalacto-transferrin


substrate_name: lacto-N-triose II

substrate: lacto-N-triose II


organism: Allomeiothermus silvanus


substrate_name: UDPgalactose

proof_lines: reaction with glucose, wild-type enzyme and N-deglycosylated recombinant enzyme

substrate: UDPgalactose


substrate_name: D-glucose

proof_lines:
recombinant enzyme
recombinant N-deglycosylated enzyme

substrate: D-glucose


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: phenyl beta-D-galactoside

substrate: phenyl beta-D-galactoside


substrate_name: di-N-acetylchitobiose

enzyme: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate: di-N-acetylchitobiose


proof_lines: using beta-Galf-(1->5)-beta-Galf-(1->6)-beta-Galf-octyl as cosubstrate, in 50 mM MOPS pH 7.6 with 20 mM MgCl2, 5 mM 2-mercaptoethanol, at 37°C

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


proof_lines: using beta-Galf-(1->6)-beta-Galf-(1->5)-beta-Galf-octyl as cosubstrate, in 50 mM MOPS pH 7.6 with 20 mM MgCl2, 5 mM 2-mercaptoethanol, at 37°C

proof_lines: spectrophotometric assay, in 50 mM MOPS, pH 7.9, 50 mM KCl, 20 mM MgCl2, at 37°C


proof_lines:
GalNAc-T2
+/-0.002 mM, pH7.4
pH 7.4, 37°C, enzyme form pp-GalNAc-T15


substrate_name: UDP-Gal

substrate: UDP-Gal


organism: Mus musculus


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Rattus norvegicus

substrate_name: UDP-N-acetyl-D-galactosamine

substrate: UDP-N-acetyl-D-galactosamine


substrate_name: GTTPSPVPTTS-(O-GalNAc)T-SAP

proof_lines:
pH 7.0, 37°C
enzyme form ppGaNTase-1
enzyme form ppGaNTase-T5

substrate: GTTPSPVPTTS-(O-GalNAc)T-SAP


organism: Streptomyces sp.

substrate_name: novobiocic acid

proof_lines: pH 6.0, temperature not specified in the publication

substrate: novobiocic acid


organism: Oryctolagus cuniculus


substrate_name: GTTPSPVPTTSTTSAP

substrate: GTTPSPVPTTSTTSAP


substrate_name: cyanidin 3-O-beta-D-glucoside

substrate: cyanidin 3-O-beta-D-glucoside


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


substrate_name: PPDAATAAPL

proof_lines: +/-0.05 mM, truncated wild-type P-T1/delta42

proof_lines: +/-0.3 mM, truncated wild-type P-T1/delta42

proof_lines: +/-0.7 mM, mutant W316Y, 38.5 times higher than wild-type

substrate: PPDAATAAPL


substrate_name: UDP-GalNAc

proof_lines: +/-0.8 mM, truncated wild-type P-T1/delta42

proof_lines: +/-0.6 mM, mutant F325L, 1.2 times higher than wild-type

proof_lines: +/-0.1 mM, mutant W316Y, 1.8 times higher than wild-type

substrate: UDP-GalNAc


enzyme_display_name: citrate (Si)-synthase

organism: Sus scrofa

substrate_name: oxaloacetate

enzyme: citrate (Si)-synthase

substrate: oxaloacetate


substrate_name: acetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA


organism: Toxoplasma gondii


enzyme_display_name: UniProt Q5XA29

organism: Streptococcus pyogenes

substrate_name: uridine

enzyme: UniProt Q5XA29

substrate: uridine


enzyme_display_name: UniProt A0A410UCT3

organism: Phytophthora capsici

enzyme: UniProt A0A410UCT3


enzyme_display_name: UniProt G4VGH9

organism: Schistosoma mansoni

substrate_name: thymidine

enzyme: UniProt G4VGH9

substrate: thymidine


enzyme_display_name: UniProt Q16831

organism: Homo sapiens

enzyme: UniProt Q16831


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: UniProt P07650

organism: Escherichia coli

enzyme: UniProt P07650


enzyme_display_name: UniProt P19971

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P19971


substrate_name: 2-deoxy-alpha-D-ribose 1-phosphate

substrate: 2-deoxy-alpha-D-ribose 1-phosphate


substrate_name: thymine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.6

substrate: thymine


enzyme_display_name: UniProt Q57VC7

organism: Trypanosoma brucei brucei

enzyme: UniProt Q57VC7


substrate_name: adenine

substrate: adenine


enzyme_display_name: nucleoside deoxyribosyltransferase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V11A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

enzyme: nucleoside deoxyribosyltransferase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V11S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt Q967M2

organism: Giardia intestinalis

enzyme: UniProt Q967M2


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


substrate_name: diphosphate

substrate: diphosphate


substrate_name: AMP

substrate: AMP


enzyme_display_name: UniProt Q97W95

organism: Saccharolobus solfataricus

enzyme: UniProt Q97W95


proof_lines:
Raw SKiD Env: Temp=60°C, pH=4.1
Raw SKiD Env: Temp=36°C, pH=7.9


enzyme_display_name: hypoxanthine phosphoribosyltransferase

organism: Streptomyces cyanogenus

substrate_name: hypoxanthine

enzyme: hypoxanthine phosphoribosyltransferase

substrate: hypoxanthine


substrate_name: guanine

substrate: guanine


enzyme_display_name: UniProt P20035

organism: Plasmodium falciparum

substrate_name: IMP

enzyme: UniProt P20035

substrate: IMP


enzyme_display_name: UniProt Q07010

enzyme: UniProt Q07010


enzyme_display_name: UniProt Q5SLS3

organism: Thermus thermophilus

enzyme: UniProt Q5SLS3