substrate_name: 2-aminoethanesulfonic acid

column_label: Table 1 part B; row 2-aminoethanesulfonic acid; column Km (mM) raw value 18.9; column kcat (s^-1) raw value 14.8; column kcat/Km (M^-1 s^-1) raw value (7.8 +/- 0.3) x 10^2

normalized_value_unit_evidence: kcat normalized_value=14.8 normalized_unit=s^-1; Km normalized_value=18.9 normalized_unit=mM; kcat/Km normalized_value=0.78 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=14.8 raw_unit=s^-1; Km raw_value=18.9 raw_unit=mM; kcat/Km raw_value=(7.8 +/- 0.3) x 10^2 raw_unit=M^-1*s^-1

row_label: 2-aminoethanesulfonic acid / PhnO Table 1 part B

substrate: 2-aminoethanesulfonic acid


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 2-aminoethyl phosphonic acid

source_db: oed

verification_status: verified

ki_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.

smiles: NCCP(=O)(O)O

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates; substrate row 2-Aminoethyl phosphonic acid; columns kcat (s^-1), Km (mM), kcat/Km (M^-1 s^-1); cells 9.0 +/- 0.2 s^-1; 1.8 +/- 0.1 mM; (5.0 +/- 0.2) x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=9.0 normalized_unit=s^-1; Km normalized_value=1.8 normalized_unit=mM; kcat/Km normalized_value=5.0 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=5.0 s^-1*mM^-1

row_label: PhnO / 2-Aminoethyl phosphonic acid

data_origin: experimental

substrate: 2-aminoethyl phosphonic acid

status: verified

source: oed


substrate_name: 3-aminopropyl phosphonic acid

verification_status: corrected

smiles: NCCCP(=O)(O)O

column_label: Table 1 part B; row 3-aminopropyl phosphonic acid; column Km (mM) raw value 4.0; column kcat (s^-1) raw value 5.4; column kcat/Km (M^-1 s^-1) raw value (1.4 +/- 0.1) x 10^3

normalized_value_unit_evidence: kcat normalized_value=5.4 normalized_unit=s^-1; Km normalized_value=4.0 normalized_unit=mM; kcat/Km normalized_value=1.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5.4 raw_unit=s^-1; Km raw_value=4.0 raw_unit=mM; kcat/Km raw_value=(1.4 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: 3-aminopropyl phosphonic acid / PhnO Table 1 part B

table_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates

substrate: 3-aminopropyl phosphonic acid

status: corrected


substrate_name: 4-aminobutylphosphonic acid

smiles: NCCCCP(=O)(O)O

column_label: Table 1 part B; row 4-aminobutylphosphonic acid; column Km (mM) raw value 13.0; column kcat (s^-1) raw value 0.5; column kcat/Km (M^-1 s^-1) raw value (3.8 +/- 0.4) x 10^1

normalized_value_unit_evidence: kcat normalized_value=0.5 normalized_unit=s^-1; Km normalized_value=13.0 normalized_unit=mM; kcat/Km normalized_value=0.038 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.5 raw_unit=s^-1; Km raw_value=13.0 raw_unit=mM; kcat/Km raw_value=(3.8 +/- 0.4) x 10^1 raw_unit=M^-1*s^-1

row_label: 4-aminobutylphosphonic acid / PhnO Table 1 part B

substrate: 4-aminobutylphosphonic acid


substrate_name: acetyl-CoA

kcat_over_km_origin: calculated

column_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates; substrate row Acetyl-CoA; columns kcat (s^-1), Km (mM), kcat/Km (M^-1 s^-1); cells 13.1 +/- 0.1 s^-1; 0.06 +/- 0.01 mM; (2.2 +/- 0.3) x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=13.1 normalized_unit=s^-1; Km normalized_value=0.06 normalized_unit=mM; kcat/Km normalized_value=218.33333333333334 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=220.0 s^-1*mM^-1

row_label: PhnO / Acetyl-CoA

substrate: acetyl-CoA


substrate_name: (aminomethyl)phosphonate

column_label: Table 1 part B; row (aminomethyl)phosphonate; column Km (mM) raw value 1.7; column kcat (s^-1) raw value 7.0; column kcat/Km (M^-1 s^-1) raw value (4.1 +/- 0.2) x 10^3

normalized_value_unit_evidence: kcat normalized_value=7.0 normalized_unit=s^-1; Km normalized_value=1.7 normalized_unit=mM; kcat/Km normalized_value=4.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7.0 raw_unit=s^-1; Km raw_value=1.7 raw_unit=mM; kcat/Km raw_value=(4.1 +/- 0.2) x 10^3 raw_unit=M^-1*s^-1

row_label: (aminomethyl)phosphonate / PhnO Table 1 part B

substrate: (aminomethyl)phosphonate


substrate_name: malonyl-CoA

column_label: Table 1 part A; row malonyl-CoA; column Km (mM) raw value 0.05; column kcat (s^-1) raw value 0.4; column kcat/Km (M^-1 s^-1) raw value (8.0 +/- 0.6) x 10^3

normalized_value_unit_evidence: kcat normalized_value=0.4 normalized_unit=s^-1; Km normalized_value=0.05 normalized_unit=mM; kcat/Km normalized_value=8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.4 raw_unit=s^-1; Km raw_value=0.05 raw_unit=mM; kcat/Km raw_value=(8.0 +/- 0.6) x 10^3 raw_unit=M^-1*s^-1

row_label: malonyl-CoA / PhnO Table 1 part A

substrate: malonyl-CoA


enzyme_display_name: gamma-glutamyltransferase

organism: Penicillium roqueforti

substrate_name: glycylglycine

source_db: brenda

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

smiles: C(C(=O)NCC(=O)O)N

enzyme: gamma-glutamyltransferase

substrate: glycylglycine

status: unverified

source: brenda


enzyme_display_name: UniProt A9YTT0

organism: Bacillus licheniformis

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A9YTT0

source: skid


organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

source_db: uniprot

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 4.70 sec(-1) with acetyl-CoA as substrate. kcat is 4.70 sec(-1) with 3-oxoadipate as substrate. kcat is 1.15 sec(-1) with beta-ketoglutarate as substrate. kcat is 0.20 sec(-1) with beta-ketohexanoate as substrate.

source: uniprot


substrate_name: propionyl-CoA

column_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates; substrate row Propionyl-CoA; columns kcat (s^-1), Km (mM), kcat/Km (M^-1 s^-1); cells 14.7 +/- 0.7 s^-1; 0.07 +/- 0.01 mM; (2.1 +/- 0.3) x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=14.7 normalized_unit=s^-1; Km normalized_value=0.07 normalized_unit=mM; kcat/Km normalized_value=209.99999999999997 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=210.0 s^-1*mM^-1

row_label: PhnO / Propionyl-CoA

substrate: propionyl-CoA


substrate_name: (S)-1-aminoethylphosphonic acid

column_label: Table 1 part B; row (S)-1-aminoethylphosphonic acid; column Km (mM) raw value 0.17; column kcat (s^-1) raw value 13.3; column kcat/Km (M^-1 s^-1) raw value (7.8 +/- 0.4) x 10^4

normalized_value_unit_evidence: kcat normalized_value=13.3 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM; kcat/Km normalized_value=78 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=13.3 raw_unit=s^-1; Km raw_value=0.17 raw_unit=mM; kcat/Km raw_value=(7.8 +/- 0.4) x 10^4 raw_unit=M^-1*s^-1

row_label: (S)-1-aminoethylphosphonic acid / PhnO Table 1 part B

substrate: (S)-1-aminoethylphosphonic acid


enzyme_display_name: ethanol O-acetyltransferase

organism: Wickerhamomyces anomalus

sequence_source: multiple

assay_conditions_summary: pH 7.5; cofactor CoA

source_databases_merged: brenda uniprot

enzyme: ethanol O-acetyltransferase


substrate_name: ethanol

smiles: CCO

substrate: ethanol


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

substrate_name: anthraniloyl-CoA

substrate: anthraniloyl-CoA


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Acinetobacter haemolyticus

substrate_name: gentamicin

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

proof_lines: S 0.5 value, Hill coefficient 2.05, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.05, pH 8.0, 37°C

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: gentamicin


substrate_name: neomycin C

proof_lines: kcat/S 0.5 value, Hill coefficient 1.43, pH 8.0, 37°C

substrate: neomycin C


substrate_name: ribostamycin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.96, pH 8.0, 37°C

substrate: ribostamycin


substrate_name: arbekacin

proof_lines: S 0.5 value, Hill coefficient 2.19, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.19, pH 8.0, 37°C

substrate: arbekacin


substrate_name: tobramicin

proof_lines: S 0.5 value, Hill coefficient 1.21, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.21, pH 8.0, 37°C

substrate: tobramicin


proof_lines: S 0.5 value, Hill coefficient 2.28, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.28, pH 8.0, 37°C


substrate_name: butirosin A

proof_lines: S 0.5 value, Hill coefficient 1.77, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.77, pH 8.0, 37°C

substrate: butirosin A


substrate_name: dibekacin

proof_lines: S 0.5 value, Hill coefficient 1.26, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.26, pH 8.0, 37°C

substrate: dibekacin


substrate_name: sisomicin

proof_lines: S 0.5 value, Hill coefficient 2.04, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.04, pH 8.0, 37°C

substrate: sisomicin


substrate_name: kanamycin B

proof_lines: S 0.5 value, Hill coefficient 1.93, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.93, pH 8.0, 37°C

substrate: kanamycin B


substrate_name: amikacin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.55, pH 8.0, 37°C

substrate: amikacin


substrate_name: isepamicin

proof_lines: S 0.5 value, Hill coefficient 1.45, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.45, pH 8.0, 37°C

substrate: isepamicin


organism: Taxus cuspidata


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Escherichia coli

substrate_name: butyryl-CoA

proof_lines: in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: butyryl-CoA


substrate_name: butirosin

substrate: butirosin


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: paromomycin

substrate: paromomycin


substrate_name: netilmicin

substrate: netilmicin


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: apramycin

substrate: apramycin


substrate_name: ribostamycin

substrate: ribostamycin


organism: Taxus sp.

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


organism: Stenotrophomonas maltophilia

substrate_name: kanamycin

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

substrate: kanamycin


substrate_name: tobramycin

substrate: tobramycin


substrate_name: neomycin

substrate: neomycin


substrate_name: arbekacin

substrate: arbekacin


organism: Pseudomonas aeruginosa

proof_lines:
reaction with AAC (6')-Ib' domain
reaction with AAC (6?)-Ib' domain


substrate_name: dibekacin

substrate: dibekacin


substrate_name: gentamicin

substrate: gentamicin


substrate_name: kanamycin A

assay_conditions_summary: pH 6

proof_lines:
reaction with AAC (6')-Ib' domain
pH 6.0
reaction with AAC (6?)-Ib' domain

substrate: kanamycin A


substrate_name: amikacin

substrate: amikacin


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines:
versus kanamycin A, K(is)
versus kanamycin A. K(is)
versus acetyl-CoA, K(is)

substrate: Unknown


organism: Homo sapiens

substrate_name: myristoyl-CoA

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

mutation_type: substitution

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: myristoyl-CoA


proof_lines:
wild-type, pH 8.0, 30°C
wild-type, pH 7.5, 25°C


enzyme_display_name: 6-deoxyerythronolide-B synthase

organism: Saccharopolyspora erythraea

substrate_name: propanoyl-CoA

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: mutant H384A, pH 7.2, temperature not specified in the publication

enzyme: 6-deoxyerythronolide-B synthase

substrate: propanoyl-CoA


proof_lines: mutant Q386E, pH 7.2, temperature not specified in the publication


proof_lines: mutant H457A, pH 7.2, temperature not specified in the publication


proof_lines: mutant N455L, pH 7.2, temperature not specified in the publication


proof_lines: mutant N381A, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, pH 7.2, temperature not specified in the publication


proof_lines: mutant T209A, pH 7.2, temperature not specified in the publication


assay_conditions_summary: pH 6.6; 298.15 K; cofactor CoA

proof_lines: pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET28a

proof_lines: pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET28a

proof_lines: pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps


proof_lines: pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b

proof_lines: pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b

proof_lines: pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b


substrate_name: neomycin B

proof_lines: in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C

substrate: neomycin B


substrate_name: sisomicin

substrate: sisomicin


enzyme_display_name: N6-hydroxylysine N-acetyltransferase

substrate_name: N-Methylhydroxylamine

smiles: CNO

enzyme: N6-hydroxylysine N-acetyltransferase

substrate: N-Methylhydroxylamine


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


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


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


substrate_name: acetyl-CoA

proof_lines:
+ L-N6-hydroxylysine
+ L-N5-hydroxyornithine
+ 1-amino-5-(hydroxyamino)pentane

substrate: acetyl-CoA


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: paromomycin

substrate: paromomycin


substrate_name: lividomycin A

substrate: lividomycin A


substrate_name: tobramycin

substrate: tobramycin


substrate_name: kanamycin B

substrate: kanamycin B


organism: Serratia marcescens

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


substrate_name: neomycin

substrate: neomycin


substrate_name: arbekacin

substrate: arbekacin


substrate_name: isepamicin

substrate: isepamicin


substrate_name: dibekacin

substrate: dibekacin


substrate_name: amikacin

substrate: amikacin


substrate_name: netilmicin

substrate: netilmicin


substrate_name: gentamicin

proof_lines:
pH 7.5
full length enzyme, pH 7.5, 25°C
isolated AAC(6') domain, pH 7.5, 25°C

substrate: gentamicin


substrate_name: kanamycin A

proof_lines:
pH 7.5
isolated AAC(6') domain, pH 7.5, 25°C
full length enzyme, pH 7.5, 25°C

substrate: kanamycin A


substrate_name: Unknown

proof_lines:
versus acetyl-CoA, K(is)
versus kanamycin A, K(is)
versus acetyl-CoA, K(ii)

substrate: Unknown


organism: Enterobacter cloacae

substrate_name: gentamicin C1

substrate: gentamicin C1


substrate_name: gentamicin C2

substrate: gentamicin C2


substrate_name: sisomicin

substrate: sisomicin


organism: Aeromonas hydrophila


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: kanamycin

substrate: kanamycin


enzyme_display_name: UniProt Q16769

substrate_name: Gln-Gln

smiles: C(CC(=O)N)C(C(=O)NC(CCC(=O)N)C(=O)O)N

assay_conditions_summary: pH 7

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=7.5

enzyme: UniProt Q16769

substrate: Gln-Gln


enzyme_display_name: UniProt Q9CYK2

organism: Mus musculus

substrate_name: L-Gln-L-Ala

smiles: CC(C(=O)O)NC(=O)C(CCC(=O)N)N

enzyme: UniProt Q9CYK2

substrate: L-Gln-L-Ala


substrate_name: L-Gln-L-Glu

smiles: C(CC(=O)N)C(C(=O)NC(CCC(=O)O)C(=O)O)N

substrate: L-Gln-L-Glu


substrate_name: L-Gln-Gly

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

substrate: L-Gln-Gly


substrate_name: L-Gln-L-Gln

substrate: L-Gln-L-Gln


organism: uncultured bacterium

proof_lines: K 0.5 value, Hill coefficient 0.62, pH 7.5, 25°C


substrate_name: gentamycin

proof_lines: K 0.5 value, Hill coefficient 3.14, pH 7.5, 25°C

substrate: gentamycin


substrate_name: tobramycin

proof_lines: K 0.5 value, Hill coefficient 2.3, pH 7.5, 25°C

substrate: tobramycin


substrate_name: acetyl-CoA

proof_lines: K 0.5 value, Hill coefficient 1.77, pH 7.5, 25°C

substrate: acetyl-CoA


proof_lines: K 0.5 value, Hill coefficient 4.39, pH 7.5, 25°C


enzyme_display_name: maltose O-acetyltransferase

assay_conditions_summary: pH 5; 323.15 K; cofactor CoA

enzyme: maltose O-acetyltransferase


substrate_name: triethanolamine

smiles: C(CO)N(CCO)CCO

substrate: triethanolamine


substrate_name: D-glucose

substrate: D-glucose


substrate_name: maltose

substrate: maltose


organism: Mycobacterium tuberculosis

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 6.8; 301.15 K; cofactor CoA

proof_lines: cosubstrate n-octanol, mutant F331H, pH 6.8, 28°C

substrate: palmitoyl-CoA


proof_lines: cosubstrate n-octanol, mutant F331Y, pH 6.8, 28°C


proof_lines: cosubstrate n-octanol, wild-type, pH 6.8, 28°C


proof_lines: cosubstrate n-octanol, mutant F331W, pH 6.8, 28°C


enzyme_display_name: 6-methylsalicylic-acid synthase

organism: Penicillium griseofulvum

substrate_name: malonyl-CoA

enzyme: 6-methylsalicylic-acid synthase

substrate: malonyl-CoA


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


organism: Enterococcus sp.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


substrate_name: neamine

substrate: neamine


substrate_name: kanamycin A

substrate: kanamycin A


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


substrate_name: diacerein

proof_lines:
transesterification, pH 5, 50°C
acetyl-CoA synthesis, pH 5, 50°C
hydrolysis of diacerein, pH 5, 50°C

substrate: diacerein


substrate_name: puerarin

proof_lines:
acetylation of puerarin, pH 5, 50°C
transesterification, pH 5, 50°C

substrate: puerarin


substrate_name: CoA

substrate: CoA


substrate_name: gentamicin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D170F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor CoA

column_label: Table 3; row D170F; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=3.4 s^-1; kcat/Km=720 s^-1 mM^-1; Km=0.0047 mM. Export values: Km=0.0047 mM; kcat=3.4 s^-1; kcat/Km=723.404 s^-1 mM^-1.

table_label: Table 3

substrate: gentamicin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D72W to reconstruct the assayed variant sequence.

column_label: Table 3; row D72W; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=3.59 s^-1; kcat/Km=190 s^-1 mM^-1; Km=0.019 mM. Export values: Km=0.019 mM; kcat=3.59 s^-1; kcat/Km=188.947 s^-1 mM^-1.


substrate_name: kanamycin

column_label: Table 4. Kinetic parameters for antibiotics; row Kanamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=4.45 s^-1; km paper=0.007 mM; kcat_over_km paper=630.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Kanamycin: kcat 4.45 s^-1; Km 7 uM (0.007 mM); kcat/Km 0.63 s^-1 uM^-1 (630.0 s^-1 mM^-1).

row_label: Kanamycin

substrate: kanamycin


substrate_name: ribostamycin

column_label: Table 4. Kinetic parameters for antibiotics; row Ribostamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=5.38 s^-1; km paper=0.0079 mM; kcat_over_km paper=680.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Ribostamycin: kcat 5.38 s^-1; Km 7.9 uM (0.0079 mM); kcat/Km 0.68 s^-1 uM^-1 (680.0 s^-1 mM^-1).

row_label: Ribostamycin

substrate: ribostamycin


substrate_name: paromomycin

column_label: Table 4. Kinetic parameters for antibiotics; row Paromomycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=5.52 s^-1; km paper=0.0067 mM; kcat_over_km paper=820.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Paromomycin: kcat 5.52 s^-1; Km 6.7 uM (0.0067 mM); kcat/Km 0.82 s^-1 uM^-1 (820.0 s^-1 mM^-1).

row_label: Paromomycin

substrate: paromomycin


substrate_name: tobramycin

column_label: Table 4. Kinetic parameters for antibiotics; row Tobramycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=5.68 s^-1; km paper=0.0066 mM; kcat_over_km paper=860.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Tobramycin: kcat 5.68 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.86 s^-1 uM^-1 (860.0 s^-1 mM^-1).

row_label: Tobramycin

substrate: tobramycin


column_label: Table 3. Enzymatic assay results between AAC(3)-IIIa mutants and gentamicin; row WT; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=6.12 s^-1; km paper=0.0071 mM; kcat_over_km paper=860.0 s^-1 mM^-1

raw_value_unit_evidence: Table 3. Enzymatic assay results between AAC(3)-IIIa mutants and gentamicin, row WT: kcat 6.12 s^-1; Km 7.1 uM (0.0071 mM); kcat/Km 0.86 s^-1 uM^-1 (860.0 s^-1 mM^-1).

row_label: WT


substrate_name: neomicin

assay_conditions_summary: pH 6.5; 295.15 K; cofactor CoA

column_label: Table 4. Kinetic parameters for antibiotics; row Neomicin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=6.15 s^-1; km paper=0.0066 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Neomicin: kcat 6.15 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.93 s^-1 uM^-1 (930.0 s^-1 mM^-1).

row_label: Neomicin

substrate: neomicin


substrate_name: sisomicin

column_label: Table 4. Kinetic parameters for antibiotics; row Sisomicin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=10.48 s^-1; km paper=0.0109 mM; kcat_over_km paper=970.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Sisomicin: kcat 10.48 s^-1; Km 10.9 uM (0.0109 mM); kcat/Km 0.97 s^-1 uM^-1 (970.0 s^-1 mM^-1).

row_label: Sisomicin

substrate: sisomicin


substrate_name: myristoyl-CoA

mutation_signature: N-terminal truncation mutant

mutation_type: truncation

proof_lines: N-terminal truncation mutant, pH 7.5, 25°C

substrate: myristoyl-CoA


substrate_name: HIV-1 negative regulatory factor

substrate: HIV-1 negative regulatory factor


smiles: CCCCCCCCO


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: 2 palmitoyl-CoA

assay_conditions_summary: pH 6.5; 310.15 K; cofactor CoA

substrate: 2 palmitoyl-CoA


substrate_name: malonyl-CoA

assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

substrate: malonyl-CoA


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


substrate_name: acetyl-CoA

proof_lines:
cosubstrate neomycin B, pH 7.6, 25°C
cosubstrate kanamycin A, pH 7.6, 25°C

substrate: acetyl-CoA


enzyme_display_name: arginine N-succinyltransferase

substrate_name: L-ornithine

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

enzyme: arginine N-succinyltransferase

substrate: L-ornithine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: Unknown

substrate: Unknown


organism: Arabidopsis thaliana


organism: Archaeoglobus fulgidus


substrate_name: formylmethanofuran

substrate: formylmethanofuran


enzyme_display_name: trihydroxystilbene synthase

organism: Arachis hypogaea

proof_lines: malonyl-CoA decarboxylation, P375G mutant enzyme

enzyme: trihydroxystilbene synthase


substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


organism: Streptomyces mobaraensis

substrate_name: hydroxylamine

substrate: hydroxylamine


substrate_name: N-CBZ-Glu-Gly

substrate: N-CBZ-Glu-Gly


organism: Solanum lycopersicum

substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

substrate: glutathione


organism: Saccharomyces cerevisiae

proof_lines:
wild-type, 37°C
His-tagged wild-type, 37°C


organism: Bos taurus


substrate_name: p60src-derived peptide

substrate: p60src-derived peptide


organism: Escherichia coli

substrate_name: tobramycin

substrate: tobramycin


substrate_name: amikacin

substrate: amikacin


enzyme_display_name: citrate (Si)-synthase

organism: Nitrobacter winogradskyi

substrate_name: oxaloacetate

enzyme: citrate (Si)-synthase

substrate: oxaloacetate


proof_lines: peptide 920 disrupts LpxA interactions with the R-3-hydroxymyristoyl-ACP substrate


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


organism: Burkholderia cepacia

substrate_name: succinyl-CoA

substrate: succinyl-CoA


enzyme_display_name: acridone synthase

organism: Citrus x microcarpa

substrate_name: N-methylanthraniloyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: product 1,3-dihydroxy-N-methylacridone, pH 7.0, 30°C

proof_lines: product 4-hydroxy-N-methylquinolone, pH 7.0, 30°C

enzyme: acridone synthase

substrate: N-methylanthraniloyl-CoA


column_label: Table 1 columns Km, kcat, and kcat/Km for row C. microcarpa ACS under 4-Coumaroyl-CoA with product Naringenin.

normalized_value_unit_evidence: Km normalized_value=0.0136 normalized_unit=mM; kcat normalized_value=0.113 normalized_unit=s^-1; kcat/Km explicit_table_normalized_value=8.333 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=13.6 +/- 3.1 raw_unit=uM; kcat raw_value=6.8 +/- 2.2 raw_unit=min^-1; kcat/Km raw_value=500 raw_unit=min^-1 mM^-1

row_label: 4-Coumaroyl-CoA / C. microcarpa ACS / Product Naringenin

table_label: Table 1. Steady-state kinetic parameters of C. microcarpa QNS and ACS


enzyme_display_name: decylcitrate synthase

organism: Talaromyces trachyspermus

substrate_name: lauroyl-CoA

enzyme: decylcitrate synthase

substrate: lauroyl-CoA


enzyme_display_name: decylhomocitrate synthase

enzyme: decylhomocitrate synthase


organism: Yarrowia lipolytica


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: Oxaloacetate; Acetyl-CoA; H2O

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

substrate: Oxaloacetate; Acetyl-CoA; H2O


enzyme_display_name: citrate (Re)-synthase

organism: Clostridium acidi-urici

substrate_name: (R)-citryl-CoA

enzyme: citrate (Re)-synthase

substrate: (R)-citryl-CoA


substrate_name: (R)-malyl-CoA

substrate: (R)-malyl-CoA


organism: Cyanidioschyzon merolae

assay_conditions_summary: pH 6.5; 321.15 K; cofactor CoA

proof_lines: without any effector, at pH 6.5 and 48°C

proof_lines: in the presence of 5 mM MgCl2, at pH 7.8 and 48°C

proof_lines: without any effector, at pH 7.8 and 48°C


enzyme_display_name: 2-methylcitrate synthase

enzyme: 2-methylcitrate synthase


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: valeryl-CoA

substrate: valeryl-CoA


enzyme_display_name: UniProt Q50I20

organism: Aspergillus fumigatus

substrate_name: CoA

enzyme: UniProt Q50I20

substrate: CoA


substrate_name: H2O; Acetyl-CoA; Oxaloacetate

assay_conditions_summary: cofactor CoA

substrate: H2O; Acetyl-CoA; Oxaloacetate


substrate_name: H2O; Oxaloacetate; Acetyl-CoA

substrate: H2O; Oxaloacetate; Acetyl-CoA


organism: Gallus gallus

substrate_name: Acetyl-CoA; H2O; Oxaloacetate

substrate: Acetyl-CoA; H2O; Oxaloacetate


organism: Rattus norvegicus


substrate_name: Acetyl-CoA; Oxaloacetate; H2O

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

substrate: Acetyl-CoA; Oxaloacetate; H2O


organism: Sus scrofa

substrate_name: oxaloacetate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H320G with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: oxaloacetate


substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H264A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 293.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D362A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F383A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: ATP citrate synthase

assay_conditions_summary: cofactor ATP

enzyme: ATP citrate synthase


substrate_name: ATP

substrate: ATP


substrate_name: citrate

substrate: citrate


substrate_name: N6-etheno-adenosine triphosphate

substrate: N6-etheno-adenosine triphosphate


column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit1p / Acetyl-CoA reports Km 76 +/- 7 uM, kcat 11.2 +/- 0.4 s^-1, and kcat/Km 150 +/- 10 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.076 mM; kcat normalized_value=11.2 s^-1; kcat/Km normalized_value=150 s^-1*mM^-1; current row stores 147.36842105263156 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=76 +/- 7 raw_unit=uM; kcat raw_value=11.2 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=150 +/- 10 raw_unit=10^3 M^-1 s^-1

row_label: Cit1p / Acetyl-CoA

table_label: Table 1


column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Acetyl-CoA reports Km 1200 +/- 200 uM, kcat 11 +/- 1 s^-1, and kcat/Km 9 +/- 2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=1.2 mM; kcat normalized_value=11 s^-1; kcat/Km normalized_value=9 s^-1*mM^-1; current row stores 9.166666666666668 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1200 +/- 200 raw_unit=uM; kcat raw_value=11 +/- 1 raw_unit=s^-1; kcat/Km raw_value=9 +/- 2 raw_unit=10^3 M^-1 s^-1

row_label: Cit3p / Acetyl-CoA


substrate_name: Propanoyl-CoA

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Propionyl-CoA reports Km 520 +/- 90 uM, kcat 5.4 +/- 0.5 s^-1, and kcat/Km 10 +/- 2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.52 mM; kcat normalized_value=5.4 s^-1; kcat/Km normalized_value=10 s^-1*mM^-1; current row stores 10.384615384615385 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=520 +/- 90 raw_unit=uM; kcat raw_value=5.4 +/- 0.5 raw_unit=s^-1; kcat/Km raw_value=10 +/- 2 raw_unit=10^3 M^-1 s^-1

row_label: Cit3p / Propionyl-CoA

substrate: Propanoyl-CoA


organism: Eimeria tenella

substrate_name: propanoyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: propanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: malate synthase

organism: Fomitopsis palustris

substrate_name: Glyoxylate; H2O; Acetyl-CoA

enzyme: malate synthase

substrate: Glyoxylate; H2O; Acetyl-CoA


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


substrate_name: glyoxalate

substrate: glyoxalate


organism: Teladorsagia circumcincta


organism: Thermus thermophilus


organism: Clostridium kluyveri

assay_conditions_summary: pH 8; cofactor CoA

column_label: Official PMC full text PMID 17400742, Determination of citrate synthase activity and Results prose for purified IPMS2/Re-citrate synthase

raw_value_unit_evidence: oxaloacetate apparent Km = 40 uM in citrate synthesis from oxaloacetate and acetyl-CoA

row_label: Oxaloacetate Km within citrate synthesis reaction using acetyl-CoA and oxaloacetate

table_label: Official PMC full text Results/prose for purified IPMS2/Re-citrate synthase


organism: Dehalococcoides mccartyi


organism: Ogataea angusta


substrate_name: glyoxylate

substrate: glyoxylate


organism: Pinus densiflora


substrate_name: Unknown

proof_lines:
enzyme form MSH
enzyme form MSL

substrate: Unknown


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Locusta migratoria

enzyme: hydroxymethylglutaryl-CoA synthase


organism: Antarctic bacterium DS2-3R

substrate_name: oxaloacetate (with propionyl-CoA at pH 8 and 23 degrees Celsius)

proof_lines: kcat is 8 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius). kcat is 21 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 23 degrees Celsius).


substrate_name: propionyl-CoA (at pH 8 and 23 degrees Celsius)


substrate_name: acetyl-CoA (at pH 8 and 23 degrees Celsius)


organism: Aspergillus nidulans


assay_conditions_summary: pH 8


organism: Homo sapiens

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

proof_lines: mutant A348G, pH 8.0, temperature not specified in the publication


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme G348G


organism: Haloferax volcanii

column_label: Table 1; HvHMGCS row; Km (uM) / Acetyl-CoA, kcat (s^-1), and kcat/Km (s^-1 mM^-1) columns; printed cells 50 +/- 6 uM, 4.6 +/- 0.2 s^-1, and 92 +/- 11 s^-1 mM^-1. Footnote a states values are means and standard errors.

raw_value_unit_evidence: Table 1 reports HvHMGCS acetyl-CoA Km = 50 +/- 6 uM, kcat = 4.6 +/- 0.2 s^-1, and kcat/Km = 92 +/- 11 s^-1 mM^-1.

row_label: HvHMGCS

table_label: Table 1. Kinetic parameters of H. volcanii, E. faecalis, and H. sapiens HMGCS enzymes


substrate_name: acetoacetyl-CoA

column_label: Table 1; HvHMGCS row; Km (uM) / Acetoacetyl-CoA column; printed cell 1.4 +/- 0.1 uM. Footnote a states values are means and standard errors.

raw_value_unit_evidence: Table 1 reports HvHMGCS acetoacetyl-CoA Km = 1.4 +/- 0.1 uM.

substrate: acetoacetyl-CoA


organism: Colwellia maris

assay_conditions_summary: 293.15 K; cofactor CoA

proof_lines:
at 20°C
at 45°C


enzyme_display_name: UniProt Q56063

organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

proof_lines: kcat is 1.4 sec(-1) for citrate synthase activity with acetyl-CoA as substrate. kcat is 1.87 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius). kcat is 7.4 sec(-1) for 2-methylcitrate syntha

source_databases_merged: skid uniprot

enzyme: UniProt Q56063


organism: Helicobacter pylori

substrate_name: H2O; Acetyl-CoA; Glyoxylate

substrate: H2O; Acetyl-CoA; Glyoxylate


enzyme_display_name: Citramalyl-CoA lyase, mitochondrial

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

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

enzyme: Citramalyl-CoA lyase, mitochondrial


substrate_name: propionyl-CoA (for beta-methylmalate synthase)


substrate_name: acetyl-CoA (for malate synthase)

substrate: acetyl-CoA (for malate synthase)


substrate_name: (S)-malyl-CoA (for malyl-CoA thioesterase activity)


organism: Gallus gallus

substrate_name: H2O; Acetoacetyl-CoA; Acetyl-CoA

substrate: H2O; Acetoacetyl-CoA; Acetyl-CoA


organism: Mus musculus


substrate_name: Coenzyme A; ATP; Citrate

substrate: Coenzyme A; ATP; Citrate


enzyme_display_name: Malate synthase G

organism: Escherichia coli (strain K12)

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: kcat is 48.1 sec(-1) for glyoxylate (at pH 8 and 37 degrees Celsius).

enzyme: Malate synthase G


organism: Euglena gracilis

proof_lines: N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25°C, pH not specified in the publication


proof_lines: wild type full-length glyoxylate cycle enzyme, at 25°C, pH not specified in the publication


enzyme_display_name: ATP-citrate synthase

organism: Rattus norvegicus

enzyme: ATP-citrate synthase


substrate_name: glyoxylate (with acetyl-CoA as cosubstrate)


substrate_name: oxaloacetate

substrate: oxaloacetate


organism: Saccharolobus solfataricus

proof_lines: pH 8.0, 70°C, native enzyme from xylose-grown cell extract


substrate_name: acetyl-CoA


organism: Enterococcus faecalis

substrate_name: Acetoacetyl-CoA; Acetyl-CoA; H2O

substrate: Acetoacetyl-CoA; Acetyl-CoA; H2O


proof_lines: kcat is 4.6 sec(-1) (at pH 8 and 30 degrees Celsius).


organism: Arthrobacter sp.

substrate_name: Propanoyl-CoA; Oxaloacetate; H2O

substrate: Propanoyl-CoA; Oxaloacetate; H2O


substrate_name: Unknown


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


substrate_name: glyoxylate

proof_lines: AceB requires a high salt concentration for activity, the optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a decrease in activity (about 2-fold).


organism: Sus scrofa

substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D375E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_variant_note: Mutation signature H274G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H274R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Citrate synthase, mitochondrial

column_label: PDF page 4, Table III, nonmutant row, Km(OAA) (uM) column = 6.0 +/- 3.7.

raw_value_unit_evidence: Table III row His274,Asp375 (nonmutant): Km(OAA) 6.0 +/- 3.7 uM.

row_label: His274,Asp375 (nonmutant)

table_label: Table III: Kinetic Parameters of Pig Citrate Synthases Expressed in E. coli

enzyme: Citrate synthase, mitochondrial


substrate_name: acetyl-coA

assay_conditions_summary: pH 8.1; cofactor CoA

column_label: PDF page 4, Table III, nonmutant row, Km(AcCoA) (uM) column = 16.3 +/- 1.5.

raw_value_unit_evidence: Table III row His274,Asp375 (nonmutant): Km(AcCoA) 16.3 +/- 1.5 uM.

substrate: acetyl-coA


organism: Escherichia coli

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.


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


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit1p / Acetyl-CoA reports Km 76 +/- 7 uM.

normalized_value_unit_evidence: Km normalized_value=0.076 mM

raw_value_unit_evidence: Km raw_value=76 +/- 7 raw_unit=uM


enzyme_display_name: Citrate synthase 3, mitochondrial

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Acetyl-CoA reports Km 1200 +/- 200 uM.

normalized_value_unit_evidence: Km normalized_value=1.2 mM

raw_value_unit_evidence: Km raw_value=1200 +/- 200 raw_unit=uM

enzyme: Citrate synthase 3, mitochondrial


substrate_name: propionyl-CoA

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Propionyl-CoA reports Km 520 +/- 90 uM.

normalized_value_unit_evidence: Km normalized_value=0.52 mM

raw_value_unit_evidence: Km raw_value=520 +/- 90 raw_unit=uM

substrate: propionyl-CoA


substrate_name: Propanoyl-CoA

sequence_variant_note: Mutation signature A361R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 8; 296.15 K; cofactor CoA

substrate: Propanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K313L/A361R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: 2-methylcitrate synthase, mitochondrial

organism: Fusarium solani

enzyme: 2-methylcitrate synthase, mitochondrial


column_label: Table 2 row Km value acetyl-CoA column McsA F. solani = 1.26 mM.

normalized_value_unit_evidence: Km normalized_value=1.26 mM

raw_value_unit_evidence: Km raw_value=1.26 raw_unit=mM

row_label: Km value acetyl-CoA / McsA F. solani

table_label: Table 2

substrate: acetyl-CoA


substrate_name: oxaloacetate (in presence of propionyl-CoA)

column_label: Table 2 row Km value oxaloacetate (propionyl-CoA) column McsA F. solani = 2.58 mM.

normalized_value_unit_evidence: Km normalized_value=2.58 mM

raw_value_unit_evidence: Km raw_value=2.58 raw_unit=mM

row_label: Km value oxaloacetate (propionyl-CoA) / McsA F. solani


enzyme_display_name: UniProt P53396

organism: Homo sapiens

substrate_name: citrate

enzyme: UniProt P53396

substrate: citrate


substrate_name: CoA

substrate: CoA


substrate_name: ATP

substrate: ATP


enzyme_display_name: Name not preserved

organism: Aspergillus fumigatus

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

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

column_label: Table 1 section Oxaloacetate; row KM (uM); mcsA column.

normalized_value_unit_evidence: 4.9 uM normalizes to 0.0049 mM, not exact exported 0.0027 mM.

raw_value_unit_evidence: Table 1 reports mcsA Oxaloacetate KM as 4.9 +/- 0.2 uM.

row_label: Oxaloacetate; KM (uM); mcsA column

table_label: Table 1: Kinetic parameters of hCS, hCSA348G, mcsA and mcsAG352A determined by UV-Vis spectroscopy

enzyme: Name not preserved


column_label: Table 2 columns Parameter and McsA A. fumigatus; row Km Oxaloacetate; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Km Oxaloacetate reports 2.7 uM in the A. fumigatus McsA column.

row_label: Km Oxaloacetate

table_label: Table 2: Comparison of properties of methylcitrate synthases from A. fumigatus and A. nidulans


column_label: Table 1 section Acetyl-CoA; row KM (uM); mcsA column.

normalized_value_unit_evidence: 5.0 uM normalizes to 0.0050 mM, not exact exported 0.0026 mM.

raw_value_unit_evidence: Table 1 reports mcsA Acetyl-CoA KM as 5.0 +/- 1.3 uM.

row_label: Acetyl-CoA; KM (uM); mcsA column


column_label: Table 2 columns Parameter and McsA A. fumigatus; row Km Acetyl-CoA; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Km Acetyl-CoA reports 2.6 uM in the A. fumigatus McsA column.

row_label: Km Acetyl-CoA


substrate_name: propanoyl-CoA

column_label: Table 1 section Propionyl-CoA; row KM (uM); mcsA column. The exported substrate spelling propanoyl-CoA is treated as the same acyl-CoA substrate label.

normalized_value_unit_evidence: 4.7 uM normalizes to 0.0047 mM, not exact exported 0.0019 mM.

raw_value_unit_evidence: Table 1 reports mcsA Propionyl-CoA KM as 4.7 +/- 0.3 uM.

row_label: Propionyl-CoA; KM (uM); mcsA column

substrate: propanoyl-CoA


column_label: Table 2 columns Parameter and McsA A. fumigatus; row Km Propionyl-CoA; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Km Propionyl-CoA reports 1.9 uM in the A. fumigatus McsA column.

row_label: Km Propionyl-CoA


organism: Chlorobaculum tepidum


organism: Gibberella moniliformis


column_label: Table 2 row Km value acetyl-CoA column McsA F. verticillioides = 2.71 mM.

normalized_value_unit_evidence: Km normalized_value=2.71 mM

raw_value_unit_evidence: Km raw_value=2.71 raw_unit=mM

row_label: Km value acetyl-CoA / McsA F. verticillioides


column_label: Table 2 row Km value oxaloacetate (propionyl-CoA) column McsA F. verticillioides = 2.81 mM.

normalized_value_unit_evidence: Km normalized_value=2.81 mM

raw_value_unit_evidence: Km raw_value=2.81 raw_unit=mM

row_label: Km value oxaloacetate (propionyl-CoA) / McsA F. verticillioides

substrate: oxaloacetate (in presence of propionyl-CoA)


organism: Hydrogenobacter thermophilus


enzyme_display_name: 2-isopropylmalate synthase

organism: Neurospora crassa

enzyme: 2-isopropylmalate synthase


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


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt P9WQB3

organism: Mycobacterium tuberculosis

substrate_name: alpha-ketoisovaleric acid

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

enzyme: UniProt P9WQB3

substrate: alpha-ketoisovaleric acid


enzyme_display_name: UniProt Q9JZG1

organism: Neisseria meningitidis

enzyme: UniProt Q9JZG1


substrate_name: alpha-Ketobutyrate

substrate: alpha-Ketobutyrate


substrate_name: alpha-ketoisovalerate

substrate: alpha-ketoisovalerate


enzyme_display_name: citrate synthase (unknown stereospecificity)

organism: Lathyrus oleraceus

substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: acetyl-CoA

enzyme: citrate synthase (unknown stereospecificity)


organism: Natronobacterium gregoryi


organism: Natronomonas pharaonis


enzyme_display_name: UniProt A4YGX6

organism: Metallosphaera sedula

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=8

enzyme: UniProt A4YGX6


enzyme_display_name: UniProt P0ABH7

proof_lines:
Raw SKiD Env: Temp=-----, pH=and
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P0ABH7


enzyme_display_name: UniProt P21553

organism: Thermoplasma acidophilum

enzyme: UniProt P21553


enzyme_display_name: UniProt P20115

organism: Arabidopsis thaliana

enzyme: UniProt P20115


organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=-----, pH=-----


organism: Yarrowia lipolytica (strain CLIB 122 / E 150)


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: valeryl-CoA

substrate: valeryl-CoA


organism: Rattus norvegicus

proof_lines:
ATP:citrate lyase
rat ACL
very similar enzymological properties


enzyme_display_name: UniProt O75390

organism: Homo sapiens

proof_lines:
human citrate synthase
catalyzes the same reaction

enzyme: UniProt O75390


enzyme_display_name: Hydroxymethylglutaryl-CoA synthase

organism: Enterococcus faecalis

enzyme: Hydroxymethylglutaryl-CoA synthase


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


enzyme_display_name: citrate (Re)-synthase

organism: Clostridium kluyveri

column_label: Official PMC full text PMID 17400742, Determination of citrate synthase activity and Results prose for purified IPMS2/Re-citrate synthase

raw_value_unit_evidence: oxaloacetate apparent Km = 40 uM

row_label: Purified IPMS2/Re-citrate synthase; oxaloacetate substrate

enzyme: citrate (Re)-synthase


raw_value_unit_evidence: acetyl-CoA apparent Km = 50 uM

row_label: Purified IPMS2/Re-citrate synthase; acetyl-CoA substrate


enzyme_display_name: homocitrate synthase

organism: Thermus thermophilus

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 323.15 K; cofactor CoA

enzyme: homocitrate synthase

substrate: Acetyl-CoA


enzyme_display_name: Citrate (Re)-synthase

organism: Dehalococcoides mccartyi (strain CBDB1)

enzyme: Citrate (Re)-synthase


organism: Syntrophus aciditrophicus


enzyme_display_name: 2-methylcitrate synthase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

column_label: Table 1 Acetyl-CoA column reports Km 265 +/- 30 uM, Kcat 1.87 +/- 0.4 s^-1, and Kcat/Km 7.05 x 10^-3; the HTML row label prints M^-1 s^-1, but the numeric row is consistent with the uM Km row and s^-1*mM^-1 export normalization

normalized_value_unit_evidence: Km normalized_value=0.265 normalized_unit=mM; Kcat normalized_value=1.87 normalized_unit=s^-1; Kcat/Km normalized_value=7.056603773584905 normalized_unit=s^-1*mM^-1 from same-table values, matching printed row after micromolar-denominator normalization

raw_value_unit_evidence: Km raw_value=265 +/- 30 raw_unit=uM; Kcat raw_value=1.87 +/- 0.4 raw_unit=s^-1; Kcat/Km raw_value=7.05 x 10^-3 raw row as printed under Kcat/Km

row_label: Acetyl-CoA column; rows Km, Kcat, and Kcat/Km

table_label: PMID 20970504 Table 1

enzyme: 2-methylcitrate synthase


column_label: Table 1 Propionyl-CoA column reports Km 45 +/- 10 uM, Kcat 8.25 +/- 0.5 s^-1, and Kcat/Km 183 x 10^-3; the HTML row label prints M^-1 s^-1, but the numeric row is consistent with the uM Km row and s^-1*mM^-1 export normalization; propanoyl-CoA and propionyl-CoA are the same acyl-CoA naming variant

normalized_value_unit_evidence: Km normalized_value=0.045 normalized_unit=mM; Kcat normalized_value=8.25 normalized_unit=s^-1; Kcat/Km normalized_value=183.33333333333334 normalized_unit=s^-1*mM^-1 from same-table values, matching printed row rounded after micromolar-denominator normalization

raw_value_unit_evidence: Km raw_value=45 +/- 10 raw_unit=uM; Kcat raw_value=8.25 +/- 0.5 raw_unit=s^-1; Kcat/Km raw_value=183 x 10^-3 raw row as printed under Kcat/Km

row_label: Propionyl-CoA column; rows Km, Kcat, and Kcat/Km


enzyme_display_name: dextrin dextranase

organism: Gluconobacter oxydans

substrate_name: maltoheptaose

enzyme: dextrin dextranase

substrate: maltoheptaose


substrate_name: maltohexaose

substrate: maltohexaose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltotriose

substrate: maltotriose


enzyme_display_name: UniProt Q1J0W0

organism: Deinococcus geothermalis

proof_lines:
Raw SKiD Env: Temp=45°C, pH=7
Raw SKiD Env: Temp=45°C, pH=5

enzyme: UniProt Q1J0W0


enzyme_display_name: Dextransucrase

organism: Leuconostoc mesenteroides

substrate_name: sucrose

sequence: DSTNTV

wild_type_sequence: DSTNTV

enzyme: Dextransucrase

substrate: sucrose


organism: Escherichia coli (strain K12)


substrate: acetyl-CoA


enzyme_display_name: Malate synthase G

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: acetyl-CoA (at pH 7.6 and 30 degrees Celsius)

enzyme: Malate synthase G


substrate_name: glyoxylate (at pH 7.6 and 30 degrees Celsius)


enzyme_display_name: Citrate synthase, mitochondrial

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Citrate synthase, mitochondrial


column_label: Downloaded ScienceDirect/EJMG PDF page 414 Table 1 lists the wild-type row with Km (uM) (Acetyl-CoA)=87.33 +/- 15, and the adjacent Results prose states Km 87.3 +/- 15 uM.

normalized_value_unit_evidence: Km normalized_value=0.0873 normalized_unit=mM from the prose value 87.3 uM.

raw_value_unit_evidence: Results prose reports Km 87.3 +/- 15 uM for wild-type mHS acetyl-CoA; Table 1 wild-type row gives Km (uM) (Acetyl-CoA)=87.33 +/- 15.

row_label: wild-type human mitochondrial HMG-CoA synthase

table_label: PDF Table 1 and adjacent Results prose


enzyme_display_name: citrate (Si)-synthase

enzyme: citrate (Si)-synthase


enzyme_display_name: Name not preserved

organism: Mycobacterium tuberculosis

enzyme: Name not preserved


substrate_name: glyoxylate

substrate: glyoxylate


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Haloferax volcanii

column_label: Table 1; HvHMGCS row; Km (uM) / Acetyl-CoA, kcat (s^-1), and kcat/Km (s^-1 mM^-1) columns; printed cells 50 +/- 6 uM, 4.6 +/- 0.2 s^-1, and 92 +/- 11 s^-1 mM^-1. Footnote a states values are means and standard errors.

raw_value_unit_evidence: Table 1 reports HvHMGCS acetyl-CoA Km = 50 +/- 6 uM, kcat = 4.6 +/- 0.2 s^-1, and kcat/Km = 92 +/- 11 s^-1 mM^-1.

row_label: HvHMGCS

enzyme: hydroxymethylglutaryl-CoA synthase


column_label: Page 8 section Activity of the Recombinant HMG-CoA Synthase states the recombinant synthase yielded a Km for Ac-CoA of 29 +/- 7 uM.

raw_value_unit_evidence: Km raw_value=29 +/- 7 raw_unit=uM

row_label: recombinant wild-type human cytoplasmic HMG-CoA synthase with Ac-CoA

table_label: Activity of the Recombinant HMG-CoA Synthase section, page 8


substrate_name: propionyl-CoA (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: propionyl-CoA (at pH 7.4)


organism: Gallus gallus


organism: Mus musculus


enzyme_display_name: malate synthase

organism: Geobacillus stearothermophilus

proof_lines:
Bacillus stearothermophilus
malate synthase
isocitrate lyase

enzyme: malate synthase


enzyme_display_name: sucrose phosphorylase

organism: Bifidobacterium dentium

substrate_name: alpha-D-glucose 1-phosphate

enzyme: sucrose phosphorylase

substrate: alpha-D-glucose 1-phosphate


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: levansucrase

organism: Pantoea agglomerans

enzyme: levansucrase


enzyme_display_name: UniProt G7LSK3

organism: Brenneria sp. EniD312

enzyme: UniProt G7LSK3


organism: Paraburkholderia graminis


enzyme_display_name: sucrose synthase

organism: Solanum tuberosum

enzyme: sucrose synthase


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: D-Xylulose

substrate: D-Xylulose


substrate_name: L-Sorbose

substrate: L-Sorbose


substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: UDP-D-glucose

substrate: UDP-D-glucose


enzyme_display_name: sucrose-phosphate synthase

organism: Ipomoea batatas

substrate_name: D-fructose 6-phosphate

enzyme: sucrose-phosphate synthase

substrate: D-fructose 6-phosphate


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Streptomyces arenae


organism: Euglena gracilis

substrate_name: acetyl-CoA


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

proof_lines:
mutant D159A
mutant D159A, acetyl-S-enzyme formation
mutant D159A, acetyl-CoA hydrolysis


proof_lines:
mutant D203A
mutant D203A, acetyl-S-enzyme formation


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


proof_lines:
mutant D99A
mutant D99A, acetyl-S-enzyme formation


organism: Escherichia coli


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

proof_lines:
wild-type, pH 8.0, 37°C
wild-type protein


substrate_name: Unknown

substrate: Unknown


organism: Aspergillus fumigatus

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme G352A


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: propanoyl-CoA

substrate: propanoyl-CoA


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


proof_lines: pH 8.0, temperature not specified in the publication, substrate: propionyl-CoA

proof_lines: pH 8.0, temperature not specified in the publication, substrate: oxaloacetate


proof_lines:
wild-type protein
wild-type, pH 8.0, 37°C


proof_lines:
pH 8.0, 25°C, purified native enzyme
versus CoA


substrate_name: CoA

proof_lines: pH 8.0, 25°C, purified native enzyme, in absence of propionyl-CoA

proof_lines: pH 8.0, 25°C, purified native enzyme, in presence of propionyl-CoA

substrate: CoA


organism: Homo sapiens

mutation_type: deletion

proof_lines: comparison of kinetic parameters measured in spectrophotometric cuvette and microplate format assays, DELTA A412 nm standard assay

proof_lines: comparison of kinetic parameters measured in spectrophotometric cuvette and microplate format assays, DELTA A412 nm microplate assay

substrate: acetyl-CoA


proof_lines: comparison of kinetic parameters measured in spectrophotometric cuvette and microplate format assays, DELTA A300 nm standard assay


proof_lines:
mutant H264A, acetyl-CoA hydrolysis
mutant H264A


proof_lines:
mutant H264N, acetyl-CoA hydrolysis
mutant H264N


organism: Bacillus sp. (in: firmicutes)


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: propionyl-CoA

substrate: propionyl-CoA


organism: Fusarium solani


proof_lines: propionyl-CoA acetyl-CoA


organism: Hevea brasiliensis


organism: Mycobacterium tuberculosis


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: ATP citrate synthase

organism: Rattus norvegicus

enzyme: ATP citrate synthase


substrate_name: phosphate

substrate: phosphate


organism: Arthrobacter sp.


organism: Bacillus anthracis


organism: Bos taurus


organism: Cupriavidus necator


organism: Enterococcus faecalis


organism: Gallus gallus

proof_lines:
acetyl-CoA hydrolysis, wild-type
wild-type, acetyl-CoA hydrolysis
wild-type, acetyl-S-enzyme formation


organism: Neurospora crassa

substrate_name: UDPglucose

substrate: UDPglucose


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


enzyme_display_name: UniProt O75795

enzyme: UniProt O75795


enzyme_display_name: UniProt P54855

substrate_name: testosterone

enzyme: UniProt P54855

substrate: testosterone


enzyme_display_name: UDP-glucuronosyltransferase 2B23

organism: Macaca fascicularis

substrate_name: androsterone

enzyme: UDP-glucuronosyltransferase 2B23

substrate: androsterone


substrate_name: estriol

substrate: estriol


enzyme_display_name: cellobiose phosphorylase

organism: Cellulomonas uda

substrate_name: D-glucoseamine

enzyme: cellobiose phosphorylase

substrate: D-glucoseamine


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


substrate_name: D-xylose

substrate: D-xylose


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


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


organism: Acetivibrio thermocellus

substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


organism: Methanosarcina barkeri


substrate_name: formylmethanofuran

substrate: formylmethanofuran


organism: Pseudomonas aeruginosa

substrate_name: acetyl-CoA


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Moraxella sp.

substrate_name: tobramycin

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: tobramycin


substrate_name: kanamycin

substrate: kanamycin


enzyme_display_name: UniProt F2RH01

organism: Streptomyces venezuelae

enzyme: UniProt F2RH01


substrate_name: ADP-glucose

substrate: ADP-glucose


substrate_name: GDP-glucose

substrate: GDP-glucose


enzyme_display_name: UniProt P16442

organism: Homo sapiens

substrate_name: UDP-N-acetylgalactosamine

enzyme: UniProt P16442

substrate: UDP-N-acetylgalactosamine


substrate_name: UDP-galactose

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

substrate: UDP-galactose


enzyme_display_name: UniProt P16422

substrate_name: UDP-alpha-D-galactose

enzyme: UniProt P16422

substrate: UDP-alpha-D-galactose


enzyme_display_name: UniProt P15291

substrate_name: chitotriose

enzyme: UniProt P15291

substrate: chitotriose


substrate_name: N-acetyl-beta-D-glucosamine

substrate: N-acetyl-beta-D-glucosamine


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

proof_lines: mutant Y130F, hydrolysis partial reaction

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetyl-CoA


enzyme_display_name: malate synthase

organism: Pseudomonas putida

substrate_name: glyoxylate

enzyme: malate synthase

substrate: glyoxylate


substrate_name: Unknown

substrate: Unknown


organism: Rhodotorula toruloides

substrate_name: ATP

substrate: ATP


substrate_name: citrate

assay_conditions_summary: buffer containing 0

proof_lines: 0.2 M Tris-HCl buffer containing 0.25 M KCl

substrate: citrate


enzyme_display_name: UniProt Q10471

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

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

enzyme: UniProt Q10471

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


substrate_name: UDP-Gal

substrate: UDP-Gal


enzyme_display_name: UniProt Q8N4A0

substrate_name: UDP-GalNAc

enzyme: UniProt Q8N4A0

substrate: UDP-GalNAc


organism: Rattus norvegicus

assay_conditions_summary: pH 7.6; buffer Hepes; cofactor ATP

proof_lines: dephosphoenzyme in Tris-HCl buffer, pH 8.7


proof_lines:
phospho-form of enzyme
dephospho-form of enzyme


organism: Saccharomyces cerevisiae

substrate_name: Gly-Asn-Ala-Ala-Ser-Arg-Arg

substrate: Gly-Asn-Ala-Ala-Ser-Arg-Arg


substrate_name: Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg

substrate: Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg


enzyme_display_name: UniProt Q93HT8

substrate_name: phenyl beta-D-glucopyranoside

enzyme: UniProt Q93HT8

substrate: phenyl beta-D-glucopyranoside


substrate_name: acetyl-CoA

assay_conditions_summary: cofactor CoA


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

substrate_name: sisomycin

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: sisomycin


substrate_name: kanamycin A

substrate: kanamycin A


organism: Mesocricetus auratus

proof_lines: pancreatic cancer cell line, distal colon


proof_lines:
distal colon
pancreatic cancer cell line


enzyme_display_name: steroid N-acetylglucosaminyltransferase

organism: Oryctolagus cuniculus

substrate_name: UDP-N-acetylglucosamine

enzyme: steroid N-acetylglucosaminyltransferase

substrate: UDP-N-acetylglucosamine


organism: Aquifex aeolicus

substrate_name: maltose

substrate: maltose


substrate_name: maltoheptaose

substrate: maltoheptaose


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltotriose

substrate: maltotriose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltohexaose

substrate: maltohexaose


organism: Ipomoea batatas


enzyme_display_name: UniProt O87172

organism: Thermus thermophilus

enzyme: UniProt O87172


enzyme_display_name: UniProt Q2VJA0

organism: Thermus brockianus

enzyme: UniProt Q2VJA0


enzyme_display_name: UniProt Q8NNA7

organism: Corynebacterium glutamicum

enzyme: UniProt Q8NNA7


enzyme_display_name: UniProt Q9LV91

organism: Arabidopsis thaliana

assay_conditions_summary: pH 7

enzyme: UniProt Q9LV91


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate: acetyl-CoA


organism: Petunia axillaris

proof_lines:
degree of polymerization: 14
degree of polymerization: 11
degree of polymerization: 7


substrate_name: UDP-D-galacturonic acid

substrate: UDP-D-galacturonic acid


organism: Nicotiana tabacum


organism: Vigna angularis


enzyme_display_name: monogalactosyldiacylglycerol synthase

organism: Bifidobacterium bifidum

substrate_name: UDPgalactose

enzyme: monogalactosyldiacylglycerol synthase

substrate: UDPgalactose


organism: Vigna radiata var. radiata


substrate_name: UDP-GalNAc

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y302L with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

substrate: UDP-GalNAc


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D458H with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: +/-0.001 mM, mutant GalNAc-T2-D458H, pH7.4


substrate_name: UDP-Gal

substrate: UDP-Gal


substrate_name: FGF23 NAPIPRRHTRSAEDDS peptide

substrate: FGF23 NAPIPRRHTRSAEDDS peptide


organism: Taeniopygia guttata


organism: Spinacia oleracea

substrate_name: UDP-D-galactose; 1,2-Diacyl-sn-glycerol

substrate: UDP-D-galactose; 1,2-Diacyl-sn-glycerol


organism: Chlorobaculum tepidum

substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Biomphalaria glabrata

substrate_name: Muc2 acceptor peptide (at pH 7 and 37 degrees Celsius)


organism: Drosophila melanogaster


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

organism: Escherichia coli

substrate_name: Galbeta-O-Me

substrate: Galbeta-O-Me


substrate_name: lactulose

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

substrate: lactulose


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus


enzyme_display_name: alpha,alpha-trehalose phosphorylase

organism: Caldanaerobacter subterraneus subsp. pacificus

substrate_name: alpha-D-arabinose

assay_conditions_summary: pH 6; 333.15 K; buffer 50 mM MES

enzyme: alpha,alpha-trehalose phosphorylase

substrate: alpha-D-arabinose


substrate_name: alpha-D-galactose

substrate: alpha-D-galactose


substrate_name: alpha-D-xylose

substrate: alpha-D-xylose


substrate_name: alpha-L-fucose

substrate: alpha-L-fucose


substrate_name: methyl beta-D-galactopyranoside

substrate: methyl beta-D-galactopyranoside


substrate_name: lactose

substrate: lactose


substrate_name: GDP-beta-L-fucose

substrate: GDP-beta-L-fucose


organism: Caldanaerobacter subterraneus

substrate_name: D-galactose

proof_lines: mutant enzyme L649G/A693Q/W371Y, at pH 6.0 and 60°C

substrate: D-galactose


substrate_name: beta-D-galactose 1-phosphate

substrate: beta-D-galactose 1-phosphate


substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


substrate_name: D-glucose

substrate: D-glucose


organism: Kocuria varians

substrate_name: trehalose

substrate: trehalose


substrate_name: phosphate

substrate: phosphate


substrate_name: glucose

substrate: glucose


enzyme_display_name: Histo-blood group ABO system transferase

substrate_name: type I H-antigen (A transferase)

proof_lines: kcat is 1.3 sec(-1) for type I H-antigen (A transferase) (PubMed:16326711). kcat is 0.5 sec(-1) for type I H-antigen (B transferase) (PubMed:16326711). kcat is 1.8 sec(-1) for type II H-antigen (A transferase) (PubMed:16326711). kcat is 1.2

substrate: type I H-antigen (A transferase)


substrate_name: IgA hinge

proof_lines: +/-0.005 mM, mutant GalNAc-T2-D458H, pH7.4

proof_lines: +/-0.006 mM, mutant GalNAc-T2-D458H, pH7.4

proof_lines: +/-0.19mM, mutant GalNAc-T2-D458H, pH7.4

substrate: IgA hinge


organism: Salisediminibacterium selenitireducens


substrate_name: alpha,alpha-trehalose

substrate: alpha,alpha-trehalose


organism: Helicobacter pylori

substrate_name: GDP-fucose

proof_lines: with Gal-beta-1,4beta-GlcNAc-O-(CH2)8CO2CH3, wild type, strain NCTC116639

substrate: GDP-fucose


proof_lines: cosubstrate: Galbeta1,3GlcNAc-O(CH2)8CO2CH3, full-length enzyme

proof_lines: with Gal-beta-1,3-GlcNAc-O-(CH2)8CO2CH3, strain UA948


organism: Euglena gracilis


organism: Ajuga reptans


substrate_name: raffinose

substrate: raffinose


mutation_signature: truncated enzyme UA948(1-428) truncated enzyme UA948(1-428)


mutation_signature: truncated enzyme UA948(1-428) cosubstrate: Galbeta1 / truncated enzyme UA948(1-428)

proof_lines: cosubstrate: Galbeta1,3GlcNAc-O(CH2)8CO2CH3, truncated enzyme UA948(1-428)


organism: Lymnaea stagnalis


organism: Caenorhabditis elegans


substrate_name: Unknown

proof_lines:
inhibition of trehalose synthesis
inhibition of trehalose phosphorolysis

substrate: Unknown


enzyme_display_name: procollagen glucosyltransferase

organism: Gallus gallus

substrate_name: D-galactosylhydroxylysine

enzyme: procollagen glucosyltransferase

substrate: D-galactosylhydroxylysine


organism: Mangifera indica


substrate_name: UDP-glucose

proof_lines: at high Mn2+-concentration, 2 Mn2+ bound

substrate: UDP-glucose


organism: Bos taurus

substrate_name: Collagen

proof_lines: denatured citrate-soluble calf skin collagen

proof_lines: acetic acid-soluble collagen from alkali-treated calf arterial tissue

substrate: Collagen


organism: Thermoanaerobacter brockii

proof_lines: kcat is 110 sec(-1) for trehalose. kcat is 110 sec(-1) for phosphate. kcat is 140 sec(-1) for D-glucose. kcat is 140 sec(-1) for beta-D-glucose 1-phosphate.


substrate_name: GDP-beta-L-fucose

substrate: GDP-beta-L-fucose


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W124R to reconstruct the assayed variant sequence.

proof_lines: mutant W124R, with Fuc-alpha-1,2Gal-beta-1,4GlcNAc-sp-biotin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W124Y to reconstruct the assayed variant sequence.

proof_lines: mutant W124Y, with Fuc-alpha-1,2Gal-beta-1,4GlcNAc-sp-biotin


proof_lines: kcat is 1.70 min(-1) for the alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc (PubMed:9737989). kcat is 9.3 min(-1) for the beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine (PubMed:9737988).


assay_conditions_summary: pH 6; buffer 50 mM MES

proof_lines: mutant enzyme R448S/N657Y, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme A440V/N657Y, in 50 mM MES buffer at pH 6.0 and 60°C


substrate_name: D-galactose

proof_lines: mutant enzyme A440M, in 50 mM MES buffer at pH 6.0 and 60°C

substrate: D-galactose


proof_lines: mutant enzyme R448D, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme R448F, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme A440E, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme N657Y, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme N657G, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme A440V/R448S, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme R448V, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme R448S, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme A440K, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme R448N, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme N657R, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme A431T, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: wild type enzyme, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme A440V, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme N657L, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme N657D, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme N657I, in 50 mM MES buffer at pH 6.0 and 60°C


proof_lines: mutant enzyme P588H, in 50 mM MES buffer at pH 6.0 and 60°C


organism: Cucurbita pepo

proof_lines:
hydrolysis
+ raffinose


substrate_name: melibiose

substrate: melibiose


proof_lines: kcat is 1.70 min(-1) for the alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc (PubMed:9737989). kcat is 9.3 min(-1) for the beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine (PubMed:9737988).


enzyme_display_name: Stachyose synthase

organism: Pisum sativum

substrate_name: galactinol

proof_lines: Vmax/KM ratio for galactosyl transfer from galactinol to stachyose is 9.5 fold higher compared with galactosyl transfer from one stachyose molecule to another.

enzyme: Stachyose synthase

substrate: galactinol


organism: Vigna angularis

proof_lines: with 1-alpha-D-galactosyl-myo-inositol at 1.1 mM

proof_lines: with galactosylononitol at nonsaturating level

proof_lines: with 1-alpha-D-galactosyl-myo-inositol at nonsaturating level


substrate_name: myo-inositol

proof_lines: with 10 mM 1-alpha-D-galactosyl-myo-inositol in the exchange reaction

substrate: myo-inositol


organism: Arabidopsis thaliana

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme


substrate_name: GDP-L-fucose

proof_lines: wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C

substrate: GDP-L-fucose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature C35T with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: Km above 0.3984 mM, isoform FUT1 mutant C35T, in 50 mM Tris-HCl (pH 7.2), at 37°C


substrate_name: alpha-D-galactosyl-D-ononitol

substrate: alpha-D-galactosyl-D-ononitol


enzyme_display_name: UniProt Q9WTS2

organism: Mus musculus

substrate_name: GDP-L-Fuc

enzyme: UniProt Q9WTS2

substrate: GDP-L-Fuc


substrate_name: phenyl-beta-D-galactoside

substrate: phenyl-beta-D-galactoside


proof_lines:
membrane-bound enzyme
recombinant LH3/GGT
calf skin collagen as acceptor


substrate_name: TDP-glucose

substrate: TDP-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D112E with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D336A to reconstruct the assayed variant sequence.

proof_lines: fucosyltransferase III mutant enzyme D336A


proof_lines: bound in purified alpha1-chain of chicken skin collagen, value based on actual amount of galactosylhydroxylysine-residues of alpha1-chain


substrate_name: phenyl-beta-D-Galactoside

substrate: phenyl-beta-D-Galactoside


organism: Rattus norvegicus

substrate_name: phenyl-beta-galactose

substrate: phenyl-beta-galactose


organism: Sus scrofa


organism: Staphylococcus aureus

substrate_name: poly(ribitol phosphate)

substrate: poly(ribitol phosphate)


organism: Staphylococcus aureus (strain COL)

substrate_name: WTA

substrate: WTA


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A431T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A431T', acceptor column group GAL; column 'Km (mM)' = 447.6; column 'kcat (s^-1)' = 66.5; column 'kcat/Km (mM^-1 s^-1)' = 0.149. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 66.5 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 66.5 s^(-1). Km: printed Table 2 cell 447.6 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 447.6 mM. kcat/Km: printed Table 2 cell 0.149 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.149 s^(-1)*mM^(-1). The exported values are kcat 66.5 s^(-1), Km 447.6 mM and kcat_over_km 0.14857015192135833 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A431T', acceptor column group GAL: Km = 447.6 mM; kcat = 66.5 s-1; printed kcat/Km = 0.149 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.

table_label: Table 2: Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes (Biotechnol. Prog., 2012, Vol. 28, No. 5, pages 1257-1262). Printed column heads: Km (mM); kcat (s^-1); kcat/Km (mM^-1 s^-1); each metric head prints one value column under the acceptor group head GLC and one under GAL.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A440E to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440E', acceptor column group GAL; column 'Km (mM)' = 68.2; column 'kcat (s^-1)' = 23.0; column 'kcat/Km (mM^-1 s^-1)' = 0.337. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.0 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 23 s^(-1). Km: printed Table 2 cell 68.2 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 68.2 mM. kcat/Km: printed Table 2 cell 0.337 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.337 s^(-1)*mM^(-1). The exported values are kcat 23.0 s^(-1), Km 68.2 mM and kcat_over_km 0.33724340175953077 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440E', acceptor column group GAL: Km = 68.2 mM; kcat = 23.0 s-1; printed kcat/Km = 0.337 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A440K to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440K', acceptor column group GAL; column 'Km (mM)' = 56.8; column 'kcat (s^-1)' = 27.7; column 'kcat/Km (mM^-1 s^-1)' = 0.488. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27.7 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 27.7 s^(-1). Km: printed Table 2 cell 56.8 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 56.8 mM. kcat/Km: printed Table 2 cell 0.488 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.488 s^(-1)*mM^(-1). The exported values are kcat 27.7 s^(-1), Km 56.8 mM and kcat_over_km 0.4876760563380282 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440K', acceptor column group GAL: Km = 56.8 mM; kcat = 27.7 s-1; printed kcat/Km = 0.488 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A440M to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440M', acceptor column group GAL; column 'Km (mM)' = 43.8; column 'kcat (s^-1)' = 17.0; column 'kcat/Km (mM^-1 s^-1)' = 0.388. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 17.0 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 17 s^(-1). Km: printed Table 2 cell 43.8 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 43.8 mM. kcat/Km: printed Table 2 cell 0.388 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.388 s^(-1)*mM^(-1). The exported values are kcat 17.0 s^(-1), Km 43.8 mM and kcat_over_km 0.3881278538812786 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440M', acceptor column group GAL: Km = 43.8 mM; kcat = 17.0 s-1; printed kcat/Km = 0.388 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A440V to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440V', acceptor column group GAL; column 'Km (mM)' = 45.7; column 'kcat (s^-1)' = 32.9; column 'kcat/Km (mM^-1 s^-1)' = 0.720. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 32.9 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 32.9 s^(-1). Km: printed Table 2 cell 45.7 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 45.7 mM. kcat/Km: printed Table 2 cell 0.720 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.72 s^(-1)*mM^(-1). The exported values are kcat 32.9 s^(-1), Km 45.7 mM and kcat_over_km 0.7199124726477023 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440V', acceptor column group GAL: Km = 45.7 mM; kcat = 32.9 s-1; printed kcat/Km = 0.720 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A440V/N657Y to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440V + N657Y', acceptor column group GAL; column 'Km (mM)' = 35.1; column 'kcat (s^-1)' = 23.6; column 'kcat/Km (mM^-1 s^-1)' = 0.672. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.6 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 23.6 s^(-1). Km: printed Table 2 cell 35.1 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 35.1 mM. kcat/Km: printed Table 2 cell 0.672 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.672 s^(-1)*mM^(-1). The exported values are kcat 23.6 s^(-1), Km 35.1 mM and kcat_over_km 0.6723646723646723 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440V + N657Y', acceptor column group GAL: Km = 35.1 mM; kcat = 23.6 s-1; printed kcat/Km = 0.672 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature A440V/R448S to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440V + R448S', acceptor column group GAL; column 'Km (mM)' = 30.1; column 'kcat (s^-1)' = 38.9; column 'kcat/Km (mM^-1 s^-1)' = 1.29. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 38.9 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 38.9 s^(-1). Km: printed Table 2 cell 30.1 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 30.1 mM. kcat/Km: printed Table 2 cell 1.29 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 1.29 s^(-1)*mM^(-1). The exported values are kcat 38.9 s^(-1), Km 30.1 mM and kcat_over_km 1.2923588039867109 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440V + R448S', acceptor column group GAL: Km = 30.1 mM; kcat = 38.9 s-1; printed kcat/Km = 1.29 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature N657D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'N657D', acceptor column group GAL; column 'Km (mM)' = 61.9; column 'kcat (s^-1)' = 35.5; column 'kcat/Km (mM^-1 s^-1)' = 0.574. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 35.5 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 35.5 s^(-1). Km: printed Table 2 cell 61.9 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 61.9 mM. kcat/Km: printed Table 2 cell 0.574 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.574 s^(-1)*mM^(-1). The exported values are kcat 35.5 s^(-1), Km 61.9 mM and kcat_over_km 0.5735056542810986 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'N657D', acceptor column group GAL: Km = 61.9 mM; kcat = 35.5 s-1; printed kcat/Km = 0.574 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature N657G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'N657G', acceptor column group GAL; column 'Km (mM)' = 58.1; column 'kcat (s^-1)' = 24.0; column 'kcat/Km (mM^-1 s^-1)' = 0.413. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 24.0 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 24 s^(-1). Km: printed Table 2 cell 58.1 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 58.1 mM. kcat/Km: printed Table 2 cell 0.413 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.413 s^(-1)*mM^(-1). The exported values are kcat 24.0 s^(-1), Km 58.1 mM and kcat_over_km 0.41308089500860584 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'N657G', acceptor column group GAL: Km = 58.1 mM; kcat = 24.0 s-1; printed kcat/Km = 0.413 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8L164 and applied mutation signature N657I to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'N657I', acceptor column group GAL; column 'Km (mM)' = 53.5; column 'kcat (s^-1)' = 42.2; column 'kcat/Km (mM^-1 s^-1)' = 0.789. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 42.2 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 42.2 s^(-1). Km: printed Table 2 cell 53.5 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 53.5 mM. kcat/Km: printed Table 2 cell 0.789 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.789 s^(-1)*mM^(-1). The exported values are kcat 42.2 s^(-1), Km 53.5 mM and kcat_over_km 0.788785046728972 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'N657I', acceptor column group GAL: Km = 53.5 mM; kcat = 42.2 s-1; printed kcat/Km = 0.789 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


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


substrate_name: D-ononitol

substrate: D-ononitol


substrate_name: Unknown

substrate: Unknown


proof_lines: isoform FUT1 mutant C35T, in 50 mM Tris-HCl (pH 7.2), at 37°C


column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'WT', acceptor column group GAL; column 'Km (mM)' = 98.0; column 'kcat (s^-1)' = 32.9; column 'kcat/Km (mM^-1 s^-1)' = 0.336. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 32.9 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 32.9 s^(-1). Km: printed Table 2 cell 98.0 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 98 mM. kcat/Km: printed Table 2 cell 0.336 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.336 s^(-1)*mM^(-1). The exported values are kcat 32.9 s^(-1), Km 98.0 mM and kcat_over_km 0.3357142857142857 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'WT', acceptor column group GAL: Km = 98.0 mM; kcat = 32.9 s-1; printed kcat/Km = 0.336 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


substrate_name: D-glucose

column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A431T', acceptor column group GLC; column 'Km (mM)' = 36.8; column 'kcat (s^-1)' = 32.1; column 'kcat/Km (mM^-1 s^-1)' = 0.872. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 32.1 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 32.1 s^(-1). Km: printed Table 2 cell 36.8 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 36.8 mM. kcat/Km: printed Table 2 cell 0.872 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.872 s^(-1)*mM^(-1). The exported values are kcat 32.1 s^(-1), Km 36.8 mM and kcat_over_km 0.8722826086956523 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A431T', acceptor column group GLC: Km = 36.8 mM; kcat = 32.1 s-1; printed kcat/Km = 0.872 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.

substrate: D-glucose


column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440E', acceptor column group GLC; column 'Km (mM)' = 2.3; column 'kcat (s^-1)' = 32.7; column 'kcat/Km (mM^-1 s^-1)' = 14. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 32.7 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 32.7 s^(-1). Km: printed Table 2 cell 2.3 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.3 mM. kcat/Km: printed Table 2 cell 14 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 14 s^(-1)*mM^(-1). The exported values are kcat 32.7 s^(-1), Km 2.3 mM and kcat_over_km 14.217391304347828 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440E', acceptor column group GLC: Km = 2.3 mM; kcat = 32.7 s-1; printed kcat/Km = 14 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440K', acceptor column group GLC; column 'Km (mM)' = 2.3; column 'kcat (s^-1)' = 41.2; column 'kcat/Km (mM^-1 s^-1)' = 18. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 41.2 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 41.2 s^(-1). Km: printed Table 2 cell 2.3 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.3 mM. kcat/Km: printed Table 2 cell 18 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 18 s^(-1)*mM^(-1). The exported values are kcat 41.2 s^(-1), Km 2.3 mM and kcat_over_km 17.91304347826087 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440K', acceptor column group GLC: Km = 2.3 mM; kcat = 41.2 s-1; printed kcat/Km = 18 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440M', acceptor column group GLC; column 'Km (mM)' = 2.1; column 'kcat (s^-1)' = 27.4; column 'kcat/Km (mM^-1 s^-1)' = 13. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27.4 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 27.4 s^(-1). Km: printed Table 2 cell 2.1 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.1 mM. kcat/Km: printed Table 2 cell 13 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 13 s^(-1)*mM^(-1). The exported values are kcat 27.4 s^(-1), Km 2.1 mM and kcat_over_km 13.047619047619046 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440M', acceptor column group GLC: Km = 2.1 mM; kcat = 27.4 s-1; printed kcat/Km = 13 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440V', acceptor column group GLC; column 'Km (mM)' = 1.9; column 'kcat (s^-1)' = 42.0; column 'kcat/Km (mM^-1 s^-1)' = 22. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 42.0 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 42 s^(-1). Km: printed Table 2 cell 1.9 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 1.9 mM. kcat/Km: printed Table 2 cell 22 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 22 s^(-1)*mM^(-1). The exported values are kcat 42.0 s^(-1), Km 1.9 mM and kcat_over_km 22.105263157894736 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440V', acceptor column group GLC: Km = 1.9 mM; kcat = 42.0 s-1; printed kcat/Km = 22 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.


column_label: Table 2 (Kinetic Parameters for Glucose and Galactose of Wild-Type Trehalose Phosphorylase and Variant Enzymes), printed body row 'A440V + N657Y', acceptor column group GLC; column 'Km (mM)' = 0.6; column 'kcat (s^-1)' = 16.1; column 'kcat/Km (mM^-1 s^-1)' = 27. The number printed beside each of these cells is that cell's own printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 16.1 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 16.1 s^(-1). Km: printed Table 2 cell 0.6 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.6 mM. kcat/Km: printed Table 2 cell 27 in a column headed kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 27 s^(-1)*mM^(-1). The exported values are kcat 16.1 s^(-1), Km 0.6 mM and kcat_over_km 26.833333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed body row 'A440V + N657Y', acceptor column group GLC: Km = 0.6 mM; kcat = 16.1 s-1; printed kcat/Km = 27 in a column headed kcat/Km (mM^-1 s^-1). The number printed beside each of these three cells is that cell's own printed uncertainty and is not a kinetic metric the export schema carries.