organism: Pyrobaculum calidifontis

substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


enzyme_display_name: carboxylesterase

organism: Pyrococcus furiosus

substrate_name: 4-methylumbelliferyl heptanoate

source_db: skid

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY-NC-ND 4.0

km_unit: mM

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

enzyme: carboxylesterase

substrate: 4-methylumbelliferyl heptanoate

source: skid


organism: Saccharolobus shibatae

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl caprylate

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

substrate: 4-nitrophenyl caprylate


organism: Sulfolobus islandicus

substrate_name: 4-nitrophenyl palmitate

kcat_display: Not reported

assay_conditions_summary: pH 8

substrate: 4-nitrophenyl palmitate


organism: Sulfurisphaera tokodaii

substrate_name: 4-nitrophenyl hexanoate

proof_lines:
Raw SKiD Env: Temp=70°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: 4-nitrophenyl hexanoate


organism: Vulcanisaeta moutnovskia

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


enzyme_display_name: dimethylnonatriene synthase

organism: Arabidopsis thaliana

substrate_name: (E,E)-geranyllinalool

source_db: uniprot

source_license: CC BY 4.0

enzyme: dimethylnonatriene synthase

substrate: (E,E)-geranyllinalool

source: uniprot


substrate_name: (3S)-(E)-Nerolidol; O2; NADPH; H+

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

sequence_source: UniProtKB:Q9LSF8 canonical sequence, reviewed entry C82G1_ARATH

assay_conditions_summary: cofactor NADPH

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

source_db: brenda

substrate: (3S)-(E)-Nerolidol; O2; NADPH; H+


organism: Zea mays

substrate_name: NADPH; O2; (3S)-(E)-Nerolidol; H+

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

sequence_source: UniProtKB:A0A1D6HSP4 canonical sequence, reviewed entry C92C5_MAIZE

substrate: NADPH; O2; (3S)-(E)-Nerolidol; H+


sequence_source: UniProtKB:A0A1D6HSP4 canonical sequence; current UniProt B6ST66 lookup redirects to A0A1D6HSP4

source: brenda


enzyme_display_name: C-19 steroid 1alpha-hydroxylase

organism: Sorangium cellulosum (strain So ce56)

substrate_name: nootkatone (in the presence of FdR_B and Fdx2)

proof_lines: kcat is 0.70 sec(-1) with nootkatone as substrate (in the presence of FdR_B and Fdx2). kcat is 0.96 sec(-1) with nootkatone as substrate (in the presence of FdR_B and Fdx8).

enzyme: C-19 steroid 1alpha-hydroxylase


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: UDP-GlcNAc

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

substrate: UDP-GlcNAc


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


organism: Sorangium cellulosum

substrate_name: testosterone

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

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda skid

substrate: testosterone


substrate_name: progesterone

sequence_source: UniProtKB:A9FDB7 plus selected source mutation note

sequence_variant_note: Mutation signature S276I matches the mutant residue at offset -4 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

mutation_type: substitution

proof_lines: pH and temperature not specified in the publication, single-mutant enzyme S276I with a truncation of the first 50 amino acid residues at the N terminus

substrate: progesterone


sequence_variant_note: Mutation signature S276N matches the mutant residue at offset +5 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH and temperature not specified in the publication, single mutant enzyme S276N with a truncation of the first 50 amino acid residues at the N terminus


sequence_source: UniProtKB:A9FDB7 plus selected source truncation note

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

mutation_type: truncation

proof_lines: pH and temperature not specified in the publication, mutant enzyme with a truncation of the first 50 amino acid residues at the N terminus


organism: Mycobacterium smegmatis


organism: Mycolicibacterium smegmatis

substrate_name: UDP-N-acetyl-D-glucosamine

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

substrate: UDP-N-acetyl-D-glucosamine


organism: Corynebacterium glutamicum

sequence_source: UniProtKB reviewed Q8NTA6; PMID 18390549; RCSB/PDBe 3C4V maps entity 1 to Q8NTA6.


enzyme_display_name: N,N'-diacetylchitobiose phosphorylase

organism: Vibrio furnissii

substrate_name: N-acetyl-D-glucosamine

sequence_source: UniProtKB reviewed accession Q9F8X1, direct REST lookup on 2026-06-30

proof_lines: pH 7.0, 30°C, reverse phosphorolysis reaction

enzyme: N,N'-diacetylchitobiose phosphorylase

substrate: N-acetyl-D-glucosamine


organism: Vibrio proteolyticus

substrate_name: N,N'-diacetylchitobiose

sequence_source: UniProtKB reviewed accession Q76IQ9, direct REST lookup on 2026-06-30

proof_lines:
pH 7.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7

substrate: N,N'-diacetylchitobiose


enzyme_display_name: lycopaoctaene synthase

organism: Botryococcus braunii

substrate_name: geranylgeranyl diphosphate

enzyme: lycopaoctaene synthase

substrate: geranylgeranyl diphosphate


source_db: oed

kcat_over_km_origin: calculated

data_origin: experimental

source: oed


enzyme_display_name: pyridoxamine-phosphate transaminase

organism: Clostridium butyricum

substrate_name: pyridoxamine 5'-phosphate

proof_lines: cosubstrate pyridoxamine 5-phosphate, pH 8.0, 37°C

enzyme: pyridoxamine-phosphate transaminase

substrate: pyridoxamine 5'-phosphate


organism: Treponema denticola

substrate_name: L-Alanine; Pyridoxal phosphate

verification_status: unverified

sequence_source: UniProtKB Q56257 canonical sequence, checked 2026-06-30; context only because the accession EC conflicts with the selected EC.

substrate: L-Alanine; Pyridoxal phosphate

status: unverified


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: D-Alanine

substrate: D-Alanine


enzyme_display_name: ribonuclease M5

organism: Bacillus subtilis

substrate_name: 5S-rRNA precursor; H2O

sequence_source: UniProtKB:P37547 direct REST lookup

enzyme: ribonuclease M5

substrate: 5S-rRNA precursor; H2O


substrate_name: artificial 5S rRNA precursor substrate in complex with BL16 subunit


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed accession O88488 (PTPRQ_RAT), direct REST check on 2026-06-30; CRC64 F0FA703022EB25D5; length 2302.


organism: Ciona intestinalis

substrate_name: phosphatidylinositol 3,4-bisphosphate

proof_lines: pH not specified in the publication, 23°C, Vmax: 0.121 nmol/min/microgram

substrate: phosphatidylinositol 3,4-bisphosphate


organism: Homo sapiens

substrate_name: Inositol 1,3,4,5-tetrakisphosphate

substrate: Inositol 1,3,4,5-tetrakisphosphate


organism: Arabidopsis thaliana

substrate_name: p-NPP

substrate: p-NPP


substrate_name: PtdIns(3,4,5)P3; 1D-myo-inositol 1,3,4-trisphosphate; 1D-myo-inositol 1,3,4,5-tetrakisphosphate; 1D-myo-inositol 1,3,4,5,6-pentakisphosphate


organism: Brassica oleracea

assay_conditions_summary: pH 5; 310.15 K; buffer ammonium acetate

proof_lines: in ammonium acetate buffer, pH 5.0, at 37°C


organism: Lilium longiflorum


sequence_source: UniProtKB reviewed accession Q5H7P5 direct REST lookup on 2026-06-30; UniProtKB reviewed (Swiss-Prot); Lilium longiflorum; Mannosylglycoprotein endo-beta-mannosidase; EC 3.2.1.152.


enzyme_display_name: 1,2-dihydroxynaphthalene dioxygenase

organism: Pseudomonas putida

sequence_source: UniProtKB:P11861 reviewed Swiss-Prot entry NAHC1_PSEPU, cross-checked against PMID 7204331 and strain NCIMB 9816/DSM 8368/PG evidence.

enzyme: 1,2-dihydroxynaphthalene dioxygenase


organism: Sphingobium xenophagum

substrate_name: O2; Naphthalene-1,2-diol

sequence_source: UniProtKB reviewed entry P74836

substrate: O2; Naphthalene-1,2-diol


verification_status: corrected

assay_conditions_summary: pH 5.5; buffer acetic acid-NaOH

proof_lines: Under alkaline conditions (pH 11), the cleavage of 1,2-DHN yield cis-2'-hydroxybenzalpyruvate.

status: corrected


enzyme_display_name: kievitone hydratase

organism: Fusarium solani

substrate_name: xanthohumol

enzyme: kievitone hydratase

substrate: xanthohumol


sequence_source: UniProtKB C7ZKN4 context only


organism: Nectria haematococca

substrate_name: H2O; Xanthohumol

sequence_source: UniProtKB C7ZKN4 context from SABIO-RK token (C7ZKN4)*2

substrate: H2O; Xanthohumol


sequence_source: UniProtKB C7ZKN4


organism: Fusarium phaseoli

substrate_name: Kievitone

substrate: Kievitone


enzyme_display_name: 7-methylxanthosine synthase

organism: Coffea arabica

substrate_name: xanthosine

enzyme: 7-methylxanthosine synthase

substrate: xanthosine


substrate_name: S-Adenosyl-L-methionine; Xanthosine

sequence_source: UniProtKB reviewed entry Q9AVK0 checked 2026-06-30

substrate: S-Adenosyl-L-methionine; Xanthosine


enzyme_display_name: chalcone synthase

organism: Medicago sativa

substrate_name: Hexanoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F215S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Hexanoyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.07; column 'Km (uM)' = 4.5; column 'kcat/Km (M^-1 s^-1)' = 272.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Hexanoyl-CoA: kcat = 0.07 min^-1; Km = 4.5 uM; printed kcat/Km = 272 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Hexanoyl-CoA'

table_label: Table 2. Steady-state kinetic parameters (Proc. Natl. Acad. Sci. U.S.A. 2002, 99(8): 5319-5324, journal page 5321)

enzyme: chalcone synthase

substrate: Hexanoyl-CoA


substrate_name: N-Methylanthraniloyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'N-methylanthraniloyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.09; column 'Km (uM)' = 3.0; column 'kcat/Km (M^-1 s^-1)' = 500.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row N-methylanthraniloyl-CoA: kcat = 0.09 min^-1; Km = 3.0 uM; printed kcat/Km = 500 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'N-methylanthraniloyl-CoA'

substrate: N-Methylanthraniloyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'o-Coumaroyl-CoA', F265V column group; column 'kcat (min^-1)' = 0.47; column 'Km (uM)' = 4.0; column 'kcat/Km (M^-1 s^-1)' = 1,958.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row o-Coumaroyl-CoA: kcat = 0.47 min^-1; Km = 4.0 uM; printed kcat/Km = 1,958 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'o-Coumaroyl-CoA'


substrate_name: butanoyl-CoA

verification_status: verified

sequence_source: UniProtKB REST accession P30074 canonical sequence

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Butyryl-CoA; literal cells kcat 0.91 min^-1, Km 4.2 uM, kcat/Km 3,611 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 0.91 min^-1 normalizes to 0.015166666666666667 s^-1 and is stored at current precision as 0.015; printed Km 4.2 uM normalizes to 0.004200000000000001 mM and is stored as 0.004; current stored quotient is 3.75 s^-1*mM^-1; the independently printed ratio normalizes to 3.611 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Butyryl-CoA: kcat 0.91 min^-1; Km 4.2 uM; kcat/Km 3,611 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Butyryl-CoA

substrate: butanoyl-CoA

status: verified


substrate_name: heptanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Heptanoyl-CoA; literal cells kcat 3.03 min^-1, Km 4.0 uM, kcat/Km 12,625 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 3.03 min^-1 normalizes to 0.050499999999999996 s^-1 and is stored at current precision as 0.051; printed Km 4.0 uM normalizes to 0.004 mM and is stored as 0.004; current stored quotient is 12.749999999999998 s^-1*mM^-1; the independently printed ratio normalizes to 12.625 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Heptanoyl-CoA: kcat 3.03 min^-1; Km 4.0 uM; kcat/Km 12,625 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Heptanoyl-CoA

substrate: heptanoyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row m-Coumaroyl-CoA; literal cells kcat 3.50 min^-1, Km 4.5 uM, kcat/Km 12,963 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 3.50 min^-1 normalizes to 0.058333333333333334 s^-1 and is stored at current precision as 0.058; printed Km 4.5 uM normalizes to 0.0045 mM and is stored as 0.005; current stored quotient is 11.6 s^-1*mM^-1; the independently printed ratio normalizes to 12.963 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row m-Coumaroyl-CoA: kcat 3.50 min^-1; Km 4.5 uM; kcat/Km 12,963 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | m-Coumaroyl-CoA


substrate_name: Benzoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Benzoyl-CoA; literal cells kcat 1.73 min^-1, Km 2.2 uM, kcat/Km 13,106 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 1.73 min^-1 normalizes to 0.028833333333333332 s^-1 and is stored at current precision as 0.029; printed Km 2.2 uM normalizes to 0.0022 mM and is stored as 0.002; current stored quotient is 14.5 s^-1*mM^-1; the independently printed ratio normalizes to 13.106 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Benzoyl-CoA: kcat 1.73 min^-1; Km 2.2 uM; kcat/Km 13,106 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Benzoyl-CoA

substrate: Benzoyl-CoA


organism: Physcomitrium patens

substrate_name: p-Coumaroyl-CoA

sequence_source: UniProtKB REST accession Q2VAZ3 canonical sequence

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

proof_lines:
37°C, pH 7.2
Raw SKiD Env: Temp=37°C, pH=7.2

substrate: p-Coumaroyl-CoA


organism: Polygonum cuspidatum

substrate_name: malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession H9DV62 canonical sequence with R105Q substitution(s) applied and applied mutation signature R105Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication

substrate: malonyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession H9DV62 canonical sequence with Q82P substitution(s) applied and applied mutation signature Q82P to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession H9DV62 canonical sequence with Q82P/C198F substitution(s) applied and applied mutation signature Q82P/C198F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication


organism: Sorbus aucuparia

substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

sequence_source: UniProtKB REST accession Q27Z06 canonical sequence

assay_conditions_summary: cofactor CoA

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


enzyme_display_name: Chalcone synthase 1

organism: Glycine max

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30 and applied mutation signature R58A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R58A, pH and temperature not specified in the publication

enzyme: Chalcone synthase 1


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30 and applied mutation signature K55A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K55A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30 and applied mutation signature K268A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K268A, pH and temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30

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


organism: Humulus lupulus


enzyme_display_name: Chalcone synthase H1

sequence_source: UniProtKB reviewed accession Q9FEY5 (CHSH1_HUMLU); fetched by UniProt REST direct accession lookup on 2026-06-30

enzyme: Chalcone synthase H1


enzyme_display_name: Chalcone synthase 2

sequence_source: UniProtKB reviewed accession P30074 (CHS2_MEDSA); fetched by UniProt REST direct accession lookup on 2026-06-30

enzyme: Chalcone synthase 2


substrate_name: Octanoyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Octanoyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.04; column 'Km (uM)' = 4.8; column 'kcat/Km (M^-1 s^-1)' = 150.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Octanoyl-CoA: kcat = 0.04 min^-1; Km = 4.8 uM; printed kcat/Km = 150 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Octanoyl-CoA'

substrate: Octanoyl-CoA


substrate_name: phenylpropionyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row '3-Phenylpropionyl-CoA', F265V column group; column 'kcat (min^-1)' = 4.40; column 'Km (uM)' = 13.8; column 'kcat/Km (M^-1 s^-1)' = 5,314.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row 3-Phenylpropionyl-CoA: kcat = 4.40 min^-1; Km = 13.8 uM; printed kcat/Km = 5,314 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row '3-Phenylpropionyl-CoA'

substrate: phenylpropionyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Hexanoyl-CoA; literal cells kcat 2.52 min^-1, Km 4.1 uM, kcat/Km 10,243 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 2.52 min^-1 normalizes to 0.042 s^-1 and is stored at current precision as 0.042; printed Km 4.1 uM normalizes to 0.0040999999999999995 mM and is stored as 0.004; current stored quotient is 10.5 s^-1*mM^-1; the independently printed ratio normalizes to 10.243 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Hexanoyl-CoA: kcat 2.52 min^-1; Km 4.1 uM; kcat/Km 10,243 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Hexanoyl-CoA


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Hexanoyl-CoA', F265V column group; column 'kcat (min^-1)' = 3.56; column 'Km (uM)' = 5.0; column 'kcat/Km (M^-1 s^-1)' = 11,866.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Hexanoyl-CoA: kcat = 3.56 min^-1; Km = 5.0 uM; printed kcat/Km = 11,866 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Hexanoyl-CoA'


substrate_name: Phenylacetyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Phenylacetyl-CoA', F265V column group; column 'kcat (min^-1)' = 4.37; column 'Km (uM)' = 5.7; column 'kcat/Km (M^-1 s^-1)' = 12,778.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Phenylacetyl-CoA: kcat = 4.37 min^-1; Km = 5.7 uM; printed kcat/Km = 12,778 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Phenylacetyl-CoA'

substrate: Phenylacetyl-CoA


substrate_name: Feruloyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Feruloyl-CoA; literal cells kcat 1.04 min^-1, Km 5.2 uM, kcat/Km 3,333 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 1.04 min^-1 normalizes to 0.017333333333333333 s^-1 and is stored at current precision as 0.017; printed Km 5.2 uM normalizes to 0.0052 mM and is stored as 0.005; current stored quotient is 3.4000000000000004 s^-1*mM^-1; the independently printed ratio normalizes to 3.333 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Feruloyl-CoA: kcat 1.04 min^-1; Km 5.2 uM; kcat/Km 3,333 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Feruloyl-CoA

substrate: Feruloyl-CoA


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Feruloyl-CoA', F265V column group; column 'kcat (min^-1)' = 2.43; column 'Km (uM)' = 9.0; column 'kcat/Km (M^-1 s^-1)' = 4,500.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Feruloyl-CoA: kcat = 2.43 min^-1; Km = 9.0 uM; printed kcat/Km = 4,500 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Feruloyl-CoA'


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Octanoyl-CoA', F265V column group; column 'kcat (min^-1)' = 9.82; column 'Km (uM)' = 5.6; column 'kcat/Km (M^-1 s^-1)' = 29,226.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Octanoyl-CoA: kcat = 9.82 min^-1; Km = 5.6 uM; printed kcat/Km = 29,226 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Octanoyl-CoA'


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'p-Coumaroyl-CoA', F265V column group; column 'kcat (min^-1)' = 2.01; column 'Km (uM)' = 5.0; column 'kcat/Km (M^-1 s^-1)' = 6,700.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row p-Coumaroyl-CoA: kcat = 2.01 min^-1; Km = 5.0 uM; printed kcat/Km = 6,700 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'p-Coumaroyl-CoA'


enzyme_display_name: pyruvate kinase

organism: Ricinus communis

substrate_name: Phosphoenolpyruvate; ADP

ki_unit: mM

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines: 2 isozymes with different kinetic mechanisms

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Unknown

assay_conditions_summary: cofactor ADP


enzyme_display_name: beta-lactamase

substrate_name: H2O; Cefoxitin

enzyme: beta-lactamase

substrate: H2O; Cefoxitin


organism: Bacillus cereus

substrate_name: 6-Aminopenicillanate; H2O

sequence_source: UniProtKB:P00809 FASTA direct lookup on 2026-06-30

substrate: 6-Aminopenicillanate; H2O


organism: Klebsiella pneumoniae

substrate_name: H2O; Cephalothin

substrate: H2O; Cephalothin


organism: Amycolatopsis methanolica


organism: Arabidopsis thaliana


organism: Bos taurus


organism: Chlamydia trachomatis


organism: Corynebacterium glutamicum


organism: Escherichia coli


organism: Homo sapiens

assay_conditions_summary: pH 8; 305.15 K; cofactor ADP

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

proof_lines: Zn2+ bound to the ADP-binding site of the free enzyme, pH 7.4, 37°C


organism: Rattus norvegicus


organism: Toxoplasma gondii

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ADP

proof_lines: PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C


substrate_name: Furopenem; H2O

assay_conditions_summary: pH 6.8; 313.15 K; buffer 50 mM HEPES

proof_lines: pH 7.0, temperature not specified in the publication

substrate: Furopenem; H2O


enzyme_display_name: bacterial sulfide:quinone reductase

substrate_name: Decylubiquinone; Sulfide

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

enzyme: bacterial sulfide:quinone reductase

substrate: Decylubiquinone; Sulfide


organism: Acidithiobacillus ferrooxidans

substrate_name: decylubiquinone

proof_lines: in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication

substrate: decylubiquinone


substrate_name: Sulfide

sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature C128S to reconstruct the assayed variant sequence.

substrate: Sulfide


organism: Caldivirga maquilingensis

proof_lines: pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K

proof_lines: pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K


enzyme_display_name: phenylalanine 4-monooxygenase

substrate_name: L-phenylalanine

enzyme: phenylalanine 4-monooxygenase

substrate: L-phenylalanine


organism: Dictyostelium discoideum

sequence_source: UniProtKB REST Q54XS1 canonical sequence

assay_conditions_summary: pH 4


source_db: sabio_rk, brenda, skid

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

sequence_source: UniProtKB REST P00439 canonical sequence

proof_lines: pH 7.0, 25°C, recombinant enzyme, versus (6R)-tetrahydrobiopterin

source_databases_merged: sabio_rk brenda skid

source: sabio_rk, brenda, skid


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R408W substitution applied during review and applied mutation signature R408W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 298.15 K; buffer 100 mM Na-HEPES

proof_lines: mutant enzyme R408W, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with L348V substitution applied during review and applied mutation signature L348V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L348V, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with P416Q substitution applied during review and applied mutation signature P416Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P416Q, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


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

proof_lines: wild type enzyme, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R155H substitution applied during review and applied mutation signature R155H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R155H, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with D143G substitution applied during review and applied mutation signature D143G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D143G, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R68S substitution applied during review and applied mutation signature R68S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R68S, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R68S, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with V388M substitution applied during review and applied mutation signature V388M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme V388M, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme V388M, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with I65T substitution applied during review and applied mutation signature I65T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme I65T, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme I65T, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R261Q substitution applied during review and applied mutation signature R261Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R261Q, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with Y414C substitution applied during review and applied mutation signature Y414C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme Y414C, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as cosubstrate


substrate_name: tetrahydrobiopterin

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with Y138E substitution applied during review and applied mutation signature Y138E to reconstruct the assayed variant sequence.

substrate: tetrahydrobiopterin


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with Y138F substitution applied during review and applied mutation signature Y138F to reconstruct the assayed variant sequence.


substrate_name: L-Phenylalanine

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

substrate: L-Phenylalanine


substrate_name: L-Tryptophan

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P04176 and applied mutation signature A47G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P04176 and applied mutation signature H64N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P04176 and applied mutation signature L48V to reconstruct the assayed variant sequence.


organism: Physcomitrium patens

substrate_name: L-phenylalanine with (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate

sequence_source: source_record; direct UniProt accession check for E5KBU4 matched organism Physcomitrium patens, EC 1.14.16.1, PMID 20959559, and 394 aa sequence length

proof_lines: kcat is 1.16 sec(-1) with L-phenylalanine as substrate and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate (PubMed:20959559). kcat is 6.89 sec(-1) with L-phenylalanine as substrate and 10-formyltetrahydrofolate as cosubstrate (Pub


organism: Pinus taeda

sequence_source: source_record; direct UniProt accession check for E5KBU3 matched organism Pinus taeda, EC 1.14.16.1, PMID 20959559, and 354 aa sequence length

proof_lines: kcat is 0.132 sec(-1) with L-phenylalanine as substrate and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate (PubMed:20959559). kcat is 2.30 sec(-1) with L-phenylalanine as substrate and 10-formyltetrahydrofolate as cosubstrate (Pu

substrate: L-phenylalanine with (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate


sequence_variant_note: Resolved canonical sequence from direct_uniprot_exact_accession_reconstructed_variant and applied mutation signature Y138K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_exact_accession_reconstructed_variant and applied mutation signature Y138A to reconstruct the assayed variant sequence.


organism: Pseudomonas fluorescens


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 840; column 'Kphe (µM)' = 569; column 'V/Kphe (µM-1 min-1)' = 1.48. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q PheH': Kphe = 569 uM; Vmax for phenylalanine hydroxylation = 840 min^-1; V/Kphe = 1.48 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/Y277H/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/Y277H/V379D PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 125; column 'Kphe (µM)' = 218; column 'V/Kphe (µM-1 min-1)' = 0.57. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/Y277H/V379D PheH': Kphe = 218 uM; Vmax for phenylalanine hydroxylation = 125 min^-1; V/Kphe = 0.57 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/Y277H/V379D PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


sequence_variant_note: Resolved canonical sequence from direct_uniprot_exact_accession_reconstructed_variant and applied mutation signature V379D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/V379D PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 281; column 'Kphe (µM)' = 1080; column 'V/Kphe (µM-1 min-1)' = 0.26. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/V379D PheH': Kphe = 1080 uM; Vmax for phenylalanine hydroxylation = 281 min^-1; V/Kphe = 0.26 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/V379D PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature Y277H to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'Y277H PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 604; column 'Kphe (µM)' = 574; column 'V/Kphe (µM-1 min-1)' = 1.05. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'Y277H PheH': Kphe = 574 uM; Vmax for phenylalanine hydroxylation = 604 min^-1; V/Kphe = 1.05 uM^-1 min^-1.

row_label: Table 3, enzyme row 'Y277H PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


organism: Chromobacterium violaceum

sequence_source: UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30)

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature L101Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM HEPES-NaOH

proof_lines: mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature L101Y/W180F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature W180F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature T254A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature F258A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C


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

proof_lines: mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C


assay_conditions_summary: pH 7.4; 303.15 K; buffer 50 mM HEPES-NaOH

proof_lines: wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C

proof_lines: wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


proof_lines: mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature Y155A to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature D139N to reconstruct the assayed variant sequence.


organism: Caenorhabditis elegans


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


proof_lines: mutant enzyme I234D, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol


proof_lines: wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol


organism: Colwellia psychrerythraea 34H

proof_lines:
pH 7.0, 10°C, recombinant enzyme
pH 7.0, 25°C, recombinant enzyme


proof_lines: wild type enzyme, without preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C

proof_lines: wild type enzyme, 5 min preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C


substrate_name: L-Phe

sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature H285Q to reconstruct the assayed variant sequence.

substrate: L-Phe


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature H290Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P04176 reviewed canonical sequence retained as context only


substrate_name: phenylalanine

sequence_source: UniProtKB:P04176 reviewed canonical sequence; BRENDA EC 1.14.16.1 Rattus norvegicus accession context

substrate: phenylalanine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16N to reconstruct the assayed variant sequence.


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


substrate_name: Abz-VAA

proof_lines:
mutant Y325F, 25°C, pH 7.0
mutant enzyme Y325F, 25°C, pH 7.0

substrate: Abz-VAA


proof_lines:
mutant Y325L, 25°C, pH 7.0
mutant enzyme Y325L, 25°C, pH 7.0


mutation_signature: Asp112-Lys452 deletion mutant

mutation_type: deletion

proof_lines: Asp112-Lys452 deletion mutant, tetrameric form

proof_lines: Asp112-Lys452 deletion mutant, L-phenylalanine activated, tetrameric form

proof_lines: Asp112-Lys452 deletion mutant, lysophosphatidylcholine and phenylalanine activated, tetrameric form


mutation_signature: Gly103-Gln428 deletion mutant

proof_lines: Gly103-Gln428 deletion mutant, tetrameric form

proof_lines: Gly103-Gln428 deletion mutant, L-phenylalanine activated, dimeric form

proof_lines: Gly103-Gln428 deletion mutant, lysophosphatidylcholine activated, dimeric form


proof_lines: recombinant enzyme, L-phenylalanine activated, tetrameric form

proof_lines: recombinant enzyme, lysophosphatidylcholine and phenylalanine activated, tetrameric form


mutation_signature: Ser2-Gln428 deletion mutant

proof_lines: Ser2-Gln428 deletion mutant, tetrameric form

proof_lines: Ser2-Gln428 deletion mutant, lysophosphatidylcholine and phenylalanine activated, dimeric form

proof_lines: Ser2-Gln428 deletion mutant, L-phenylalanine activated, dimeric form


mutation_signature: truncated enzyme containing C-terminal 334 amino acids truncated enzyme containing C-terminal 334 amino acids


proof_lines: allelic combination wild-type/mutant I65T, Vmax: 1 micromol/min/mg, pH 6.8, 37°C

proof_lines: allelic combination wild-type/mutant R68S, Vmax: 1 micromol/min/mg, pH 6.8, 37°C


substrate_name: tryptophan

assay_conditions_summary: pH 7

proof_lines: truncated enzyme containing C-terminal 334 amino acids, pH 7.0

proof_lines: truncated enzyme containing C-terminal 334 amino acids, pH 8.0

substrate: tryptophan


organism: Legionella pneumophila


organism: Mus musculus

proof_lines: using 6-methyltetrahydropterin as cofactor

proof_lines: using 5,6,7,8-tetrahydrobiopterin as cofactor


substrate_name: L-phenylalanine (at 25 degrees Celsius)

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

substrate: L-phenylalanine (at 25 degrees Celsius)


organism: Pseudomonas sp.

substrate_name: Unknown

substrate: Unknown


proof_lines: phosphorylated recombinant wild-type enzyme


proof_lines: pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH V379D

proof_lines: pH 7.0, 25°C, recombinant mutant DELTA 117PheH V379D


proof_lines: pH 7.0, 25°C, recombinant mutant DELTA 117PheH

proof_lines: pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH


enzyme_display_name: leucyl aminopeptidase

organism: Unknown

enzyme: leucyl aminopeptidase


organism: Arabidopsis thaliana

substrate_name: L-leucine-p-nitroanilide

substrate: L-leucine-p-nitroanilide


organism: Solanum lycopersicum


organism: Bos taurus

substrate_name: L-Leucylglycine

substrate: L-Leucylglycine


substrate_name: Cys-Gly

source_db: brenda,skid

substrate: Cys-Gly

source: brenda,skid


substrate_name: Ser-Gly

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

substrate: Ser-Gly


substrate_name: H2O; L-Cysteinylglycine

substrate: H2O; L-Cysteinylglycine


substrate_name: Met-Gly

substrate: Met-Gly


organism: Clonorchis sinensis


proof_lines:
pH 8, 20°C
pH 7.5, 37°, Vmax: 10.7 microM/min


organism: Cryptosporidium parvum


organism: Sus scrofa

substrate_name: H2O; Leu-p-nitroanilide

substrate: H2O; Leu-p-nitroanilide


substrate_name: H2O; Arg-7-amino-4-methylcoumarin

substrate: H2O; Arg-7-amino-4-methylcoumarin


substrate_name: Leu-p-nitroanilide

substrate: Leu-p-nitroanilide


organism: Thermotoga maritima


organism: Trypanosoma cruzi


proof_lines:
pH 9.0, 50°C
native enzyme, pH 7.5, 37°C
recombinant enzyme, pH 7.5, 37°C


organism: Desulfurococcus amylolyticus

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

proof_lines: pH 7.5, 50°C, enzyme activated by heating at 70°C


organism: Geobacillus kaustophilus

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q7X2C8 and applied mutation signature N345L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 20 mM Tris-HCl

proof_lines: mutant enzyme N345L, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2


proof_lines: wild type enzyme, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q7X2C8 and applied mutation signature N345Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N345Q, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2


organism: Haemaphysalis longicornis


organism: Leishmania amazonensis

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme


organism: Leishmania donovani


organism: Leishmania major


organism: Plasmodium berghei


organism: Acinetobacter calcoaceticus

substrate_name: leucinamide

substrate: leucinamide


organism: Aspergillus oryzae


proof_lines:
Zn2+-Zn2+-enzyme form
similar value
lens enzyme


organism: Cannabis sativa


organism: Eisenia fetida


organism: Gadus morhua


organism: Gallus gallus


organism: Hippoglossus hippoglossus


organism: Homo sapiens


organism: Hordeum vulgare

substrate_name: H2O; Leu-Tyr

substrate: H2O; Leu-Tyr


organism: Lactobacillus acidophilus

substrate_name: L-Leu-Gly

substrate: L-Leu-Gly


organism: Bos taurus

substrate_name: Cys-Gly (at pH 6.9 and 25 degrees Celsius)

proof_lines: kcat is 3400 min(-1) for Cys-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 11500 min(-1) for Leu-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 8150 min(-1) for Met-Gly hydrolysis activity (at pH 6


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: H-Leu-NHMec (in the presence of Zn(2+), but only metal binding site 2 occupied)

assay_conditions_summary: pH 8

proof_lines: kcat is 2200 sec(-1) with for H-Leu-NHMec as substrate (in the presence of Zn(2+), but only metal binding site 2 occupied) (PubMed:19408962). kcat is 3800 sec(-1) with for H-Leu-NHMec as substrate (in the presence of Zn(2+), both metal bind


organism: Plasmodium vivax (strain Salvador I)

substrate_name: H-Leu-NHMec

proof_lines: kcat is 0.04 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:34133730). kcat is 0.98 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the prese

substrate: H-Leu-NHMec


organism: Solanum lycopersicum

substrate_name: Leu-Gly

proof_lines: kcat is 120 sec(-1) with Leu-Gly as substrate.

substrate: Leu-Gly


organism: Lingulaulax polyedra


organism: Morimus funereus


organism: Pagrus major

assay_conditions_summary: pH 7; 310.15 K; buffer 25 mM sodium phosphate

proof_lines: in 25 mM sodium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol and 0.02% NaN3, at 37°C


organism: Phaseolus vulgaris

substrate_name: Ala-Ala-Ala-Ala

substrate: Ala-Ala-Ala-Ala


organism: Plasmodium falciparum

proof_lines: pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2


organism: Plasmodium vivax


organism: Schistosoma mansoni


organism: Setaria cervi


substrate_name: Gly-Gly

proof_lines:
His-tagged recombinant enzyme, 37°C
free recombinant enzyme, 37°C

substrate: Gly-Gly


organism: Acanthamoeba castellanii


organism: Arabidopsis thaliana

substrate_name: H2O; L-Leucinyl-p-nitroanilide

substrate: H2O; L-Leucinyl-p-nitroanilide


substrate_name: L-Cysteinylglycine

substrate: L-Cysteinylglycine


substrate_name: Cys-Leu

substrate: Cys-Leu


substrate_name: H2O; L-Cysteinylglycine


substrate_name: Leu-Cys

substrate: Leu-Cys


organism: Babesia gibsoni


proof_lines: pH 8.0, 37°C, recombinant GST-tagged enzyme


organism: Bacillus subtilis


proof_lines: inhibitory activity against recombinant enzyme


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Pseudoalteromonas agarivorans

substrate_name: L-Leu 7-amido-4-methylcoumarin

substrate: L-Leu 7-amido-4-methylcoumarin


organism: Salmonella enterica

substrate_name: Asp-Phe

substrate: Asp-Phe


organism: Schizosaccharomyces pombe


substrate_name: Leu-p-nitroanilide


substrate_name: Arg-Leu

substrate: Arg-Leu


smiles: NCC(O)=NCC(=O)O


substrate_name: Leu-Leu

substrate: Leu-Leu


substrate_name: Glycyl-leucine

substrate: Glycyl-leucine


substrate_name: Arg-Gly

substrate: Arg-Gly


substrate_name: Leu-Gly-Gly

substrate: Leu-Gly-Gly


substrate_name: Arg-Gly-Asp

substrate: Arg-Gly-Asp


substrate_name: Arg-Gly-Phe

substrate: Arg-Gly-Phe


substrate_name: H2O; Leu-Gly

substrate: H2O; Leu-Gly


substrate_name: L-Leucylglycine

substrate: L-Leucylglycine


organism: Solanum tuberosum


organism: Staphylococcus aureus


organism: Sus scrofa

substrate_name: Gly-Phe

proof_lines:
Zn2+-Zn2+-enzyme form
Mg2+-Zn2+-enzyme form
native enzyme, pH 8.0, 25°C

substrate: Gly-Phe


organism: Telchin licus licus

proof_lines: pH 7.0, temperature not specified in the publication


organism: Thermomyces lanuginosus


organism: Toxoplasma gondii


organism: Vibrio proteolyticus


enzyme_display_name: beta-glucosidase

organism: Oryza sativa subsp. japonica

substrate_name: p-nitrophenyl beta-D-glucoside (at pH 5.0)

enzyme: beta-glucosidase


substrate: p-nitrophenyl beta-D-glucoside (at pH 5.0)


organism: Phanerodontia chrysosporium

substrate_name: cellobiose

substrate: cellobiose


organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)


organism: Zea mays

substrate_name: p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)


organism: Halothermothrix orenii

sequence_source: UniProtKB:B8CYA8 direct REST lookup; active primary accession B8CYA8

assay_conditions_summary: pH 7; 343.15 K; buffer the coupled glucose oxidase/peroxidase method in 20 mM HEPES

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'WT', D-cellobiose block: k_cat,app = 387 ± 15; K_m = 10.0 ± 1.0; k_cat,app/K_m = 38.7.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 387 ± 15 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 387.0 s^(-1). K_m: printed Table 2 cell 10.0 ± 1.0 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 10.0 mM. k_cat/K_m: printed Table 2 cell 38.7 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 38.7 s^(-1)*mM^(-1). Closure check: 387.0 / 10.0 = 38.7 s^-1 mM^-1, which rounds to the printed efficiency cell 38.7 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'WT', D-cellobiose block: column 'k_cat,app (s^-1)' prints 387 ± 15; column 'K_m (mM)' prints 10.0 ± 1.0; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 38.7.

row_label: Table 2, body row 'WT' (wild type (the unmarked 70 °C row)), D-cellobiose block


substrate_name: lactose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature F417Y to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'F417Y', D-lactose block: k_cat,app = 41.5 ± 1.2; K_m = 10.3 ± 0.9; k_cat,app/K_m = 4.0.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 41.5 ± 1.2 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 41.5 s^(-1). K_m: printed Table 2 cell 10.3 ± 0.9 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 10.3 mM. k_cat/K_m: printed Table 2 cell 4.0 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 4.0 s^(-1)*mM^(-1). Closure check: 41.5 / 10.3 = 4.02913 s^-1 mM^-1, which rounds to the printed efficiency cell 4.0 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'F417Y', D-lactose block: column 'k_cat,app (s^-1)' prints 41.5 ± 1.2; column 'K_m (mM)' prints 10.3 ± 0.9; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 4.0.

row_label: Table 2, body row 'F417Y' (variant F417Y), D-lactose block

substrate: lactose


organism: Homo sapiens

sequence_source: UniProtKB:Q9H227 direct REST lookup; active primary accession Q9H227


organism: Hordeum vulgare

substrate_name: H2O; Sophorose

sequence_source: UniProtKB:Q40025 direct REST lookup; active primary accession Q40025

substrate: H2O; Sophorose


organism: Lamium galeobdolon


substrate_name: oleuropein

substrate: oleuropein


substrate_name: Dhurrin

substrate: Dhurrin


organism: Listeria innocua Clip11262

sequence_source: UniProtKB:Q92AS9 direct REST lookup; active primary accession Q92AS9


substrate_name: sophorotetraose

assay_conditions_summary: pH 6; 293.15 K; buffer 50 mM Mes

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Sop4: kcat (s^-1) = 3.5 ± 0.9; Km (mM) = 10 ± 4; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 0.34 ± 0.04.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.5 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 3.5 s^(-1). Km: printed Table 1 cell 10 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 10.0 mM. kcat/Km: printed Table 1 cell 0.34 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.34 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Sop4: kcat = 3.5 ± 0.9 s^-1; Km = 10 ± 4 mM; printed kcat/Km = 0.34 ± 0.04 s^-1 mM^-1.

table_label: Table 1: Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc (PLoS ONE 2016, 11(2))

substrate: sophorotetraose


substrate_name: laminaribiose

sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB:Q92AS9 canonical sequence by applying R572K and applied mutation signature R572K to reconstruct the assayed variant sequence.

substrate: laminaribiose


substrate_name: Laminaripentaose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Lam5: kcat (s^-1) = 12 ± 5; Km (mM) = 5.5 ± 2.8; Kis (mM) = 2.7 ± 1.6; kcat/Km (s^-1 mM^-1) = 2.1 ± 0.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 12 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 12.0 s^(-1). Km: printed Table 1 cell 5.5 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 5.5 mM. kcat/Km: printed Table 1 cell 2.1 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 2.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Lam5: kcat = 12 ± 5 s^-1; Km = 5.5 ± 2.8 mM; printed kcat/Km = 2.1 ± 0.2 s^-1 mM^-1.

substrate: Laminaripentaose


substrate_name: laminaritriose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Lam3: kcat (s^-1) = 11 ± 1; Km (mM) = 3.7 ± 0.3; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 2.9 ± 0.1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 11 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 11.0 s^(-1). Km: printed Table 1 cell 3.7 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 3.7 mM. kcat/Km: printed Table 1 cell 2.9 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 2.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Lam3: kcat = 11 ± 1 s^-1; Km = 3.7 ± 0.3 mM; printed kcat/Km = 2.9 ± 0.1 s^-1 mM^-1.

substrate: laminaritriose


substrate_name: sophorose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q92AS9 and applied mutation signature R572K to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the R572K enzyme block, substrate row Sop2: kcat (s^-1) = 15 ± 1; Km (mM) = 21 ± 2; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 0.69 ± 0.03.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 15.0 s^(-1). Km: printed Table 1 cell 21 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 21.0 mM. kcat/Km: printed Table 1 cell 0.69 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.69 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, R572K enzyme block, substrate row Sop2: kcat = 15 ± 1 s^-1; Km = 21 ± 2 mM; printed kcat/Km = 0.69 ± 0.03 s^-1 mM^-1.

substrate: sophorose


substrate_name: sophoropentaose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Sop5: kcat (s^-1) = 1.0 ± 0.4; Km (mM) = 11 ± 6; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 0.098 ± 0.020.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.0 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 1.0 s^(-1). Km: printed Table 1 cell 11 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 11.0 mM. kcat/Km: printed Table 1 cell 0.098 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.098 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Sop5: kcat = 1.0 ± 0.4 s^-1; Km = 11 ± 6 mM; printed kcat/Km = 0.098 ± 0.020 s^-1 mM^-1.

substrate: sophoropentaose


organism: Thermotoga neapolitana

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB:Q0GC07 direct REST lookup

substrate: 4-nitrophenyl beta-D-glucopyranoside


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

sequence_source: UniProtKB:B9K7M5 direct REST lookup

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


organism: Triticum aestivum

substrate_name: H2O; Luteolin 7-O-beta-D-glucoside

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

substrate: H2O; Luteolin 7-O-beta-D-glucoside


substrate_name: HBOA glucoside; H2O

substrate: HBOA glucoside; H2O


substrate_name: H2O; Apigenin 7-O-beta-D-glucoside

substrate: H2O; Apigenin 7-O-beta-D-glucoside


substrate_name: H2O; p-Nitrophenyl-beta-D-fucoside

substrate: H2O; p-Nitrophenyl-beta-D-fucoside


substrate_name: H2O; p-Nitrophenyl-beta-D-glucoside

sequence_source: UniProtKB:Q1XIR9 direct REST lookup

substrate: H2O; p-Nitrophenyl-beta-D-glucoside


sequence_source: UniProtKB:Q1XH04 direct REST lookup

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1c', pNP-Glc block; column 'Km (mM)' = 1.75; column 'kcat (s^-1)' = 235.9; column 'kcat/Km (s^-1/mM)' = 135.

normalized_value_unit_evidence: kcat: printed Table II cell 235.9 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 235.9 s^(-1). Km: printed cell 1.75 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 1.75 mM. kcat/Km: printed cell 135 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 135.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1c, pNP-Glc block: Km cell 1.75 mM; kcat cell 235.9 s^-1; printed kcat/Km cell 135 s^-1/mM.

row_label: Table II, row TaGlu1c, pNP-Glc block


sequence_source: UniProtKB:Q1XH05 direct REST lookup

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1b', pNP-Glc block; column 'Km (mM)' = 2.16; column 'kcat (s^-1)' = 128.2; column 'kcat/Km (s^-1/mM)' = 59.3.

normalized_value_unit_evidence: kcat: printed Table II cell 128.2 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 128.2 s^(-1). Km: printed cell 2.16 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 2.16 mM. kcat/Km: printed cell 59.3 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 59.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1b, pNP-Glc block: Km cell 2.16 mM; kcat cell 128.2 s^-1; printed kcat/Km cell 59.3 s^-1/mM.

row_label: Table II, row TaGlu1b, pNP-Glc block


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-fucopyranoside

sequence_source: UniProtKB:A0A1E1FFN6 direct REST lookup

proof_lines: pH 6.0, 60°C, additive: 25 mM cellobiose

proof_lines: pH 6.0, 60°C, additive: 250 mM D-galactose

substrate: 4-nitrophenyl beta-D-fucopyranoside


sequence_source: UniProtKB:Q41761 direct REST lookup


substrate_name: Dhurrin; H2O

sequence_source: UniProtKB:P49235 direct REST lookup

substrate: Dhurrin; H2O


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=5.8


substrate_name: DIBOA-beta-D-glucoside (with native hexamer)

proof_lines: kcat is 48.8 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 338 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 99.2 sec(-1) with p-nitrophenyl beta-D-glucopyranoside


proof_lines: kcat is 137 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 773 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 235.9 sec(-1) with p-nitrophenyl beta-D-glucopyranoside

substrate: DIBOA-beta-D-glucoside (with native hexamer)


proof_lines: kcat is 214 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 1201 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 128.2 sec(-1) with p-nitrophenyl beta-D-glucopyranosid


proof_lines: kcat is 5728 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 330 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme).


organism: Prunus dulcis

substrate_name: beta-Methyl-D-glucopyranoside; H2O

proof_lines: enzyme immobilized on polysulphone capillary membranes, at pH 6.5 and 25°C

proof_lines: increased Km if enzyme immobilized on cellulose

substrate: beta-Methyl-D-glucopyranoside; H2O


organism: Raphanus sativus


organism: Rattus norvegicus


organism: Sinapis alba


organism: Sulfolobus solfataricus


organism: Thermosphaera aggregans


sequence_source: UniProtKB exact accession Q92AS9

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Lam2: kcat (s^-1) = 23 ± 1; Km (mM) = 2.7 ± 0.2; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 8.8 ± 0.4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 23.0 s^(-1). Km: printed Table 1 cell 2.7 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 2.7 mM. kcat/Km: printed Table 1 cell 8.8 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 8.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Lam2: kcat = 23 ± 1 s^-1; Km = 2.7 ± 0.2 mM; printed kcat/Km = 8.8 ± 0.4 s^-1 mM^-1.


substrate_name: laminaritetraose

substrate: laminaritetraose


substrate_name: sophorotriose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Sop3: kcat (s^-1) = 56 ± 11; Km (mM) = 15 ± 4; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 3.8 ± 0.3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 56 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 56.0 s^(-1). Km: printed Table 1 cell 15 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 15.0 mM. kcat/Km: printed Table 1 cell 3.8 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 3.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Sop3: kcat = 56 ± 11 s^-1; Km = 15 ± 4 mM; printed kcat/Km = 3.8 ± 0.3 s^-1 mM^-1.

substrate: sophorotriose


substrate_name: sophorotetraose

substrate: sophorotetraose


organism: Oryza sativa

sequence_source: UniProtKB exact accession Q75I93


substrate_name: H2O; N-Heptyl-beta-D-glucoside

substrate: H2O; N-Heptyl-beta-D-glucoside


sequence_source: UniProtKB exact accession Q8L7J2


sequence_source: UniProtKB exact accession A3BMZ5


sequence_source: UniProtKB exact accession Q75I94


organism: Phanerochaete chrysosporium

substrate_name: H2O; Cellobiose

sequence_source: UniProtKB exact accession Q25BW4

substrate: H2O; Cellobiose


sequence_source: UniProtKB exact accession Q25BW5


organism: Pyrococcus furiosus

sequence_source: UniProtKB exact accession Q51723


organism: Secale cereale

sequence_source: UniProtKB exact accession Q9FYS3


organism: Sorghum bicolor

sequence_source: UniProtKB exact accession Q41290


organism: Spodoptera frugiperda

substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_source: UniProtKB exact accession O61594

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: 2-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB exact accession Q9YGA8

substrate: 2-nitrophenyl beta-D-glucopyranoside


organism: Acetivibrio thermocellus


enzyme_display_name: Beta-glucosidase 45

organism: Arabidopsis thaliana

substrate_name: H2O; Coniferin

enzyme: Beta-glucosidase 45

substrate: H2O; Coniferin


enzyme_display_name: Beta-glucosidase 46

enzyme: Beta-glucosidase 46


enzyme_display_name: Myrosinase 5

enzyme: Myrosinase 5


enzyme_display_name: Myrosinase 4

enzyme: Myrosinase 4


enzyme_display_name: Myrosinase 1

enzyme: Myrosinase 1


enzyme_display_name: Beta-glucosidase BoGH3A

organism: Bacteroides ovatus

substrate_name: H2O; Cellotetraose

enzyme: Beta-glucosidase BoGH3A

substrate: H2O; Cellotetraose


enzyme_display_name: Beta-glucosidase BoGH3B

enzyme: Beta-glucosidase BoGH3B


organism: Bifidobacterium breve


organism: Cellulomonas fimi

substrate_name: p-Nitrophenyl-beta-D-glucoside; H2O

substrate: p-Nitrophenyl-beta-D-glucoside; H2O


enzyme_display_name: Beta-glucosidase

organism: Halothermothrix orenii

substrate_name: lactose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature Y296F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'Y296F', D-lactose block: k_cat,app = 6.9 ± 0.2; K_m = 29.1 ± 2.3; k_cat,app/K_m = 0.24.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 6.9 ± 0.2 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 6.9 s^(-1). K_m: printed Table 2 cell 29.1 ± 2.3 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 29.1 mM. k_cat/K_m: printed Table 2 cell 0.24 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.24 s^(-1)*mM^(-1). Closure check: 6.9 / 29.1 = 0.237113 s^-1 mM^-1, which rounds to the printed efficiency cell 0.24 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'Y296F', D-lactose block: column 'k_cat,app (s^-1)' prints 6.9 ± 0.2; column 'K_m (mM)' prints 29.1 ± 2.3; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 0.24.

row_label: Table 2, body row 'Y296F' (variant Y296F), D-lactose block

enzyme: Beta-glucosidase

substrate: lactose


column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'WT', D-lactose block: k_cat,app = 366 ± 17; K_m = 26.3 ± 2.8; k_cat,app/K_m = 13.9.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 366 ± 17 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 366.0 s^(-1). K_m: printed Table 2 cell 26.3 ± 2.8 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 26.3 mM. k_cat/K_m: printed Table 2 cell 13.9 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 13.9 s^(-1)*mM^(-1). Closure check: 366.0 / 26.3 = 13.9163 s^-1 mM^-1, which rounds to the printed efficiency cell 13.9 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'WT', D-lactose block: column 'k_cat,app (s^-1)' prints 366 ± 17; column 'K_m (mM)' prints 26.3 ± 2.8; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 13.9.

row_label: Table 2, body row 'WT' (wild type (the unmarked 70 °C row)), D-lactose block


substrate_name: cellobiose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature N222F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'N222F', D-cellobiose block: k_cat,app = 16.9 ± 1.3; K_m = 93.2 ± 12.6; k_cat,app/K_m = 0.18.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 16.9 ± 1.3 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 16.9 s^(-1). K_m: printed Table 2 cell 93.2 ± 12.6 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 93.2 mM. k_cat/K_m: printed Table 2 cell 0.18 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.18 s^(-1)*mM^(-1). Closure check: 16.9 / 93.2 = 0.18133 s^-1 mM^-1, which rounds to the printed efficiency cell 0.18 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'N222F', D-cellobiose block: column 'k_cat,app (s^-1)' prints 16.9 ± 1.3; column 'K_m (mM)' prints 93.2 ± 12.6; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 0.18.

row_label: Table 2, body row 'N222F' (variant N222F), D-cellobiose block

substrate: cellobiose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature N294T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'N294T', D-lactose block: k_cat,app = 7.4 ± 0.2; K_m = 30.8 ± 2.0; k_cat,app/K_m = 0.24.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 7.4 ± 0.2 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 7.4 s^(-1). K_m: printed Table 2 cell 30.8 ± 2.0 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 30.8 mM. k_cat/K_m: printed Table 2 cell 0.24 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.24 s^(-1)*mM^(-1). Closure check: 7.4 / 30.8 = 0.24026 s^-1 mM^-1, which rounds to the printed efficiency cell 0.24 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'N294T', D-lactose block: column 'k_cat,app (s^-1)' prints 7.4 ± 0.2; column 'K_m (mM)' prints 30.8 ± 2.0; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 0.24.

row_label: Table 2, body row 'N294T' (variant N294T), D-lactose block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature F417S to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'F417S', D-cellobiose block: k_cat,app = 0.38 ± 0.01; K_m = 11.9 ± 0.9; k_cat,app/K_m = 0.032.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 0.38 ± 0.01 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 0.38 s^(-1). K_m: printed Table 2 cell 11.9 ± 0.9 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 11.9 mM. k_cat/K_m: printed Table 2 cell 0.032 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.032 s^(-1)*mM^(-1). Closure check: 0.38 / 11.9 = 0.0319328 s^-1 mM^-1, which rounds to the printed efficiency cell 0.032 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'F417S', D-cellobiose block: column 'k_cat,app (s^-1)' prints 0.38 ± 0.01; column 'K_m (mM)' prints 11.9 ± 0.9; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 0.032.

row_label: Table 2, body row 'F417S' (variant F417S), D-cellobiose block


column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'N294T', D-cellobiose block: k_cat,app = 16.5 ± 0.4; K_m = 9.0 ± 0.8; k_cat,app/K_m = 1.8.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 16.5 ± 0.4 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 16.5 s^(-1). K_m: printed Table 2 cell 9.0 ± 0.8 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 9.0 mM. k_cat/K_m: printed Table 2 cell 1.8 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 1.8 s^(-1)*mM^(-1). Closure check: 16.5 / 9.0 = 1.83333 s^-1 mM^-1, which rounds to the printed efficiency cell 1.8 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'N294T', D-cellobiose block: column 'k_cat,app (s^-1)' prints 16.5 ± 0.4; column 'K_m (mM)' prints 9.0 ± 0.8; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 1.8.

row_label: Table 2, body row 'N294T' (variant N294T), D-cellobiose block


substrate_name: p-nitrophenyl-beta-D-mannopyranoside

substrate: p-nitrophenyl-beta-D-mannopyranoside


substrate_name: syringin (at pH 5.5)

substrate: syringin (at pH 5.5)


substrate_name: p-coumaryl alcohol glucoside (at pH 5.5)


substrate_name: sinigrin (at pH 4.5)

substrate: sinigrin (at pH 4.5)


substrate_name: scopolin (with recombinant enzyme)

substrate: scopolin (with recombinant enzyme)


substrate_name: pNP-beta-D-glucoside

substrate: pNP-beta-D-glucoside


organism: Fulvia fulva

substrate_name: pNPG

substrate: pNPG


sequence: GVDVLLGQGLLAPRTPFTGEGPSQKSYGTELLSKPNDGK

wild_type_sequence: GVDVLLGQGLLAPRTPFTGEGPSQKSYGTELLSKPNDGK


organism: Oryza sativa subsp. japonica

substrate_name: p-nitrophenyl beta-D-glucoside (at pH 5.0)

assay_conditions_summary: pH 5


proof_lines: kcat is 1.30 sec(-1) with kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 1.10 sec(-1) with quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 0.92 sec(-1) with kaempferol 3-O-beta-glucoside as


substrate_name: pNP beta-D-glucopyranoside

proof_lines: kcat is 10.2 sec(-1) with pNP beta-D-glucopyranoside as substrate (PubMed:34965581). kcat is 12.9 sec(-1) with pNP beta-D-fucopyranoside as substrate (PubMed:34965581). kcat is 13.6 sec(-1) with pNP beta-D-galactopyranoside as substrate (Pu

substrate: pNP beta-D-glucopyranoside


organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)

proof_lines: kcat is 1.57 sec(-1) for cellobiose. kcat is 3.99 sec(-1) for cellotetraose. kcat is 4.91 sec(-1) for cellohexaose.


substrate_name: cellotetraose

proof_lines: kcat is 65.0 sec(-1) for cellotetraose. kcat is 0.62 sec(-1) for cellohexaose.

substrate: cellotetraose


organism: Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (pNPGal) (at pH 5.5 and 75 degrees Celsius)

proof_lines: kcat is 4522 sec(-1) with pNPGal as substrate. kcat is 3750.6 sec(-1) with pNPGlu as substrate. kcat is 944.3 sec(-1) with pNPC as substrate. kcat is 652.6 sec(-1) with pNPX as substrate. kcat is 2149 sec(-1) with cellobiose as substrate.


proof_lines: The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar.


organism: Homo sapiens

substrate_name: glucosylceramide (at 37 degrees Celsius and pH 6.0)

assay_conditions_summary: pH 6

proof_lines: kcat is 0.43 min(-1) for the hydrolysis of glucosylceramide (PubMed:17595169). kcat<0.01 min(-1) for the hydrolysis of galactosylceramide (PubMed:17595169). kcat is 7.26 min(-1) for the hydrolysis of C6-NBD-glucosylceramide (PubMed:17595169


substrate_name: p-nitrophenyl beta-D-glucopyranoside

proof_lines: kcat is 18.5 sec(-1) with p-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 0.27 sec(-1) with p-nitrophenyl beta-D-thioglucoside as substrate. kcat is 12.1 sec(-1) with n-heptyl-beta-D-glucoside as substrate. kcat is 9.8 sec(-1) wi

substrate: p-nitrophenyl beta-D-glucopyranoside


substrate_name: para-nitrophenyl beta-D-glucopyranoside

proof_lines: kcat is 3.82 sec(-1) with para-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 23.8 sec(-1) with para-nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.381 sec(-1) with para-nitrophenyl beta-D-xylopyranoside as substrate. k

substrate: para-nitrophenyl beta-D-glucopyranoside


proof_lines: kcat is 3.05 sec(-1) with para-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 6.92 sec(-1) with para-nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.788 sec(-1) with para-nitrophenyl beta-D-xylopyranoside as substrate. k


substrate_name: DIBOA-beta-D-glucoside

proof_lines: kcat is 172 sec(-1) with DIBOA-beta-D-glucoside as substrate. kcat is 118 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 119 sec(-1) with DIMBOA-beta-D-glucoside as substrate. kcat is 158 sec(-1) with DI

substrate: DIBOA-beta-D-glucoside


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

proof_lines: kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of cellobiose, cellotriose and cellotetraose, respectively.


enzyme_display_name: carboxylesterase

organism: Thermobifida fusca

substrate_name: p-nitrophenol acetate

enzyme: carboxylesterase

substrate: p-nitrophenol acetate


substrate_name: cis-Permethrin; H2O

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

proof_lines:
pH 7.5, 25°C
pH 7.0, 37°C, isoform CES2
pH 7.0, 37°C

substrate: cis-Permethrin; H2O


organism: Rattus norvegicus

substrate_name: trans-Permethrin; H2O

proof_lines:
hydrolase A, pH 7.4, 37°C
hydrolase B, pH 7.4, 37°C
pH 5.0, 37°C

substrate: trans-Permethrin; H2O


organism: Sus scrofa

substrate_name: H2O; 4-Nitrophenyl acetate

proof_lines:
pH 7.4, 37°C
at pH 7.4 and 37Â°C
isoenzyme V

substrate: H2O; 4-Nitrophenyl acetate


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-2'; substrate row 'A6'; column 'Km(uM)' = 2.1; column 'kcat(min-1)' = 0.34; column 'kcat/Km(uM-1 min-1)' = 0.16.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-2', substrate row 'A6': Km = 2.1 uM; kcat = 0.34 min^-1; printed kcat/Km = 0.16 uM^-1 min^-1.

table_label: Table 5: Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates (Arch Biochem Biophys 2006;445(1):115-123)


substrate_name: H2O; Carboxylic ester

substrate: H2O; Carboxylic ester


organism: Lactobacillus casei


organism: Lactococcus lactis subsp. cremoris


organism: Oryctolagus cuniculus

substrate_name: 1-R,S-cis-Permethrin; H2O

proof_lines:
isoform CES1, at pH 6.5 and 37Â°C
ratio kcat/Km is 180 per min and mM
at pH 7.4 and 37Â°C

substrate: 1-R,S-cis-Permethrin; H2O


organism: Pseudomonas aeruginosa

substrate_name: H2O; p-Nitrophenyl butyrate

substrate: H2O; p-Nitrophenyl butyrate


organism: Pseudomonas putida


organism: Pyrobaculum sp.

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


organism: Pyrococcus furiosus

substrate_name: 4-Methylumbelliferyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8TZJ1 and applied mutation signature W194A to reconstruct the assayed variant sequence.

substrate: 4-Methylumbelliferyl butyrate


substrate_name: 4-Methylumbelliferyl heptanoate

substrate: 4-Methylumbelliferyl heptanoate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8TZJ1 and applied mutation signature F198A to reconstruct the assayed variant sequence.


substrate_name: H2O; All-trans-Retinyl palmitate

substrate: H2O; All-trans-Retinyl palmitate


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl caproate

proof_lines: pH and temperature not specified in the publication

substrate: 4-nitrophenyl caproate


substrate_name: 4-nitrophenyl caprylate

column_label: Table 1 on journal page 1154, p-Nitrophenyl caprylate block, enzyme row Wild-type; column kcat/Km (s^-1 mM^-1) = 63; column Km (uM) = 28; column kcat (s^-1) = 1.7.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 1.7 s^(-1). Km: printed Table 1 cell 28 uM; 1 uM is 1/1000 mM, so 28 / 1000 = 0.028 mM. kcat/Km: printed Table 1 cell 63 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 63.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Wild-type, p-Nitrophenyl caprylate block: kcat/Km = 63 s^-1 mM^-1; Km = 28 uM; kcat = 1.7 s^-1.

table_label: Table 1: Kinetic parameters of wild-type SsoPEst and R210A (Biotechnology Letters 2010, volume 32, pages 1151-1157)

substrate: 4-nitrophenyl caprylate


column_label: Table 1 on journal page 1154, p-Nitrophenyl butyrate block, enzyme row Wild-type; column kcat/Km (s^-1 mM^-1) = 5.1; column Km (mM) = 0.93; column kcat (s^-1) = 4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 4.0 s^(-1). Km: printed Table 1 cell 0.93 mM; the printed column is already in mM, so no unit conversion applies and the value carries over as 0.93 mM. kcat/Km: printed Table 1 cell 5.1 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 5.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Wild-type, p-Nitrophenyl butyrate block: kcat/Km = 5.1 s^-1 mM^-1; Km = 0.93 mM; kcat = 4 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97VU1 and applied mutation signature R210A to reconstruct the assayed variant sequence.

column_label: Table 1 on journal page 1154, p-Nitrophenyl caprylate block, enzyme row R210A; column kcat/Km (s^-1 mM^-1) = 192; column Km (uM) = 43; column kcat (s^-1) = 7.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.8 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 7.8 s^(-1). Km: printed Table 1 cell 43 uM; 1 uM is 1/1000 mM, so 43 / 1000 = 0.043 mM. kcat/Km: printed Table 1 cell 192 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 192.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R210A, p-Nitrophenyl caprylate block: kcat/Km = 192 s^-1 mM^-1; Km = 43 uM; kcat = 7.8 s^-1.


substrate_name: 5'-L-Phenylalanyl-floxuridine; H2O

substrate: 5'-L-Phenylalanyl-floxuridine; H2O


organism: Vibrio vulnificus

substrate_name: H2O; p-Nitrophenyl acetate

substrate: H2O; p-Nitrophenyl acetate


organism: Vulcanisaeta moutnovskia


organism: Actinidia eriantha

substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


organism: Arabidopsis thaliana

substrate_name: the synthetic substrate p-nitrophenyl acetate (pNPA)


organism: Felis catus

substrate_name: p-NPA

substrate: p-NPA


organism: Geobacillus stearothermophilus

substrate_name: p-nitrophenyl caproate (at 60 degrees Celsius)


organism: Homo sapiens


substrate_name: p-nitrophenyl valerate

substrate: p-nitrophenyl valerate


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

substrate_name: p-nitrophenyl butyrate

substrate: p-nitrophenyl butyrate


organism: Rattus norvegicus


substrate_name: retinyl palmitate

substrate: retinyl palmitate


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: 4-methylumbelliferyl (4-MU) butyrate (at 37 degrees Celsius)


organism: Sus scrofa


organism: Vibrio vulnificus (strain CMCP6)

substrate_name: pNPA

proof_lines: kcat is 0.67 sec(-1) with pNPA as substrate.

substrate: pNPA


substrate_name: H2O; 4-Methylumbelliferyl acetate

sequence_source: UniProtKB direct accession lookup: Q0ZPV7

proof_lines:
pH 8.0, 25°C
Raw SKiD Env: Temp=25°C, pH=8

substrate: H2O; 4-Methylumbelliferyl acetate


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl dodecanoate; H2O

substrate: p-Nitrophenyl dodecanoate; H2O


substrate_name: Methyl indole-3-acetate; H2O

sequence_source: UniProtKB direct accession lookup: Q9SG92

substrate: Methyl indole-3-acetate; H2O


organism: Archaeoglobus fulgidus

substrate_name: Triacetin; H2O

sequence_source: UniProtKB direct accession lookup: O28558

proof_lines:
70°C, pH 7.1
pH 7.1, 50°C
Raw SKiD Env: Temp=70°C, pH=7.1

substrate: Triacetin; H2O


organism: Bacillus sp.

sequence_source: UniProtKB direct accession lookup: Q6DV85


sequence_source: UniProtKB direct accession lookup: Q6DV84


organism: Escherichia coli


organism: Felis silvestris catus

sequence_source: UniProtKB direct accession lookup: Q8I034


organism: Ferroplasma acidiphilum

substrate_name: 4-nitrophenyl butyrate

sequence_source: UniProtKB direct accession lookup: Q2PCE5

proof_lines:
pH 2.0, 50°C
Raw SKiD Env: Temp=50°C, pH=2
Raw SKiD Env: Temp=35°C, pH=6

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl hexanoate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2PCE5 and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of EstFa_R and its AQGF mutant), AQGF block, row 'pNP caproate'; column 'kcat (s^-1)' = 159 ± 4; column 'Km (mM)' = 0.13 ± 0.02; column 'kcat/Km (s^-1 mM^-1)' = 1275.

normalized_value_unit_evidence: kcat: printed Table 1 cell 159 ± 4 s^-1; the cell is already in s^-1, so no unit conversion applies, and the paper value is 159.0 s^(-1), which is the value the catalog already carries. Km: printed Table 1 cell 0.13 ± 0.02 mM; the cell is already in mM, so no unit conversion applies, and the paper value is 0.13 mM, which is the value the catalog already carries. kcat/Km: printed Table 1 cell 1275 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and the paper value is 1275.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, AQGF block, row 'pNP caproate': kcat = 159 ± 4 s^-1; Km = 0.13 ± 0.02 mM; printed kcat/Km = 1275 s^-1 mM^-1.

row_label: Table 1, AQGF (N248A/P256Q/E257G/S283F) block, row 'pNP caproate'

table_label: Table 1: Kinetic parameters of EstFa_R and its AQGF mutant (J. Biol. Chem. 2014, 289(35):24499-24510)

substrate: 4-nitrophenyl hexanoate