substrate_name: tributyrin

column_label: Table 1 (journal page 31), decoded transcription, enzyme row PLEst, substrate column group Tributyrin (C4): kcat (s^-1) = 70; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 70 s^-1 -> 70.0 s^(-1); the catalog holds 70.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 1400.0 s^(-1)*mM^(-1) is the exact quotient 70 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: tributyrin


enzyme_display_name: carboxylesterase

organism: Sus scrofa

substrate_name: Vinylacetate

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB Q29550 direct accession lookup

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

smiles: C=CCC(=O)O

column_label: Table 3 (journal page 32), decoded transcription, enzyme row PLEst, substrate column group Vinyl acetate (C2): kcat (s^-1) = 315; Km/K0.5 (mM) = 4.

normalized_value_unit_evidence: kcat: printed cell 315 s^-1 -> 315.0 s^(-1); the catalog holds 315.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 4 mM -> 4.0 mM; the catalog holds 4.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 78.75 s^(-1)*mM^(-1) is the exact quotient 315 / 4 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 3 (journal page 32) 'Kinetic parameters kcat and K0.5 of the hydrolysis of vinyl esters by members of the HSL family and other lipolytic and non-lipolytic carboxyesterases'

data_origin: experimental

enzyme: carboxylesterase

substrate: Vinylacetate

status: verified

source: oed


substrate_name: vinyl propionate

smiles: C=COC(=O)CC

column_label: Table 3 (journal page 32), decoded transcription, enzyme row PLEst, substrate column group Vinyl propionate (C3): kcat (s^-1) = 295; Km/K0.5 (mM) = 5.

normalized_value_unit_evidence: kcat: printed cell 295 s^-1 -> 295.0 s^(-1); the catalog holds 295.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 5 mM -> 5.0 mM; the catalog holds 5.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 59.0 s^(-1)*mM^(-1) is the exact quotient 295 / 5 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl propionate


substrate_name: vinyl butyrate

smiles: C=COC(=O)CCC

column_label: Table 3 (journal page 32), decoded transcription, enzyme row PLEst, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 460; Km/K0.5 (mM) = 2.

normalized_value_unit_evidence: kcat: printed cell 460 s^-1 -> 460.0 s^(-1); the catalog holds 460.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2 mM -> 2.0 mM; the catalog holds 2.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 230.0 s^(-1)*mM^(-1) is the exact quotient 460 / 2 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl butyrate


organism: Rhizomucor miehei

substrate_name: Triacetin

verification_status: unverified

kcat_over_km_display: Not reported

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

smiles: CC(=O)OCC(COC(C)=O)OC(C)=O

substrate: Triacetin

status: unverified


smiles: CCCC(=O)OCC(COC(=O)CCC)OC(=O)CCC


organism: Saccharolobus shibatae

substrate_name: 4-nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5NU42 plus Q249P/G250E reconstruction and applied mutation signature Q249P/G250E to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl butyrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5NU42 plus A241N/Q249P/G250E/F276S reconstruction and applied mutation signature A241N/Q249P/G250E/F276S to reconstruct the assayed variant sequence.


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


organism: Thermomyces lanuginosus


substrate_name: tripropionin

smiles: CCC(=O)OCC(COC(=O)CC)OC(=O)CC

substrate: tripropionin


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


substrate_name: vinyl laurate

smiles: C=COC(=O)CCCCCCCCCCC

substrate: vinyl laurate


organism: Vulcanisaeta moutnovskia

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl caprylate

sequence_source: UniProtKB Q97VU1 direct REST FASTA/JSON, sequence version 1

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.

mutation_type: substitution

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.


enzyme_display_name: acetate kinase

organism: Methanosarcina thermophila

substrate_name: Acetate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H180E to reconstruct the assayed variant sequence.

smiles: CC(=O)O

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180E', acetate column group; column 'Km (mM)' = 17; column 'kcat (s^-1)' = 702; column 'kcat/Km (mM^-1 s^-1)' = 41.

normalized_value_unit_evidence: Km: printed TABLE II cell 17 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 17.0 mM. kcat: printed TABLE II cell 702 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 702.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 41 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 41.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180E', acetate column group: Km = 17 mM; kcat = 702 s^-1; printed kcat/Km = 41 mM^-1 s^-1.

table_label: TABLE II: Kinetic parameters of the position-180 variant acetate kinases (J. Biol. Chem. 275, 33765-33770, 2000)

enzyme: acetate kinase

substrate: Acetate


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H180Q to reconstruct the assayed variant sequence.

column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180Q', ATP column group; column 'Km (mM)' = 3.7; column 'kcat (s^-1)' = 653; column 'kcat/Km (mM^-1 s^-1)' = 176.

normalized_value_unit_evidence: Km: printed TABLE II cell 3.7 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 3.7 mM. kcat: printed TABLE II cell 653 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 653.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 176 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 176.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180Q', ATP column group: Km = 3.7 mM; kcat = 653 s^-1; printed kcat/Km = 176 mM^-1 s^-1.

substrate: ATP


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H123A to reconstruct the assayed variant sequence.

column_label: TABLE I (Kinetic parameters of acetate kinase variants obtained by replacement of conserved histidines with alanine), enzyme-form row 'H123A', acetate column group; column 'Km (mM)' = 16; column 'kcat (s^-1)' = 411; column 'kcat/Km (mM^-1 s^-1)' = 25.

normalized_value_unit_evidence: Km: printed TABLE I cell 16 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 16.0 mM. kcat: printed TABLE I cell 411 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 411.0 s^(-1). kcat/Km: Printed TABLE I kcat/Km cell 25 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 25.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE I, enzyme-form row 'H123A', acetate column group: Km = 16 mM; kcat = 411 s^-1; printed kcat/Km = 25 mM^-1 s^-1.

table_label: TABLE I: Kinetic parameters of acetate kinase variants obtained by replacement of conserved histidines with alanine (J. Biol. Chem. 275, 33765-33770, 2000)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H180N to reconstruct the assayed variant sequence.

column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180N', ATP column group; column 'Km (mM)' = 4.6; column 'kcat (s^-1)' = 761; column 'kcat/Km (mM^-1 s^-1)' = 166.

normalized_value_unit_evidence: Km: printed TABLE II cell 4.6 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 4.6 mM. kcat: printed TABLE II cell 761 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 761.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 166 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 166.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180N', ATP column group: Km = 4.6 mM; kcat = 761 s^-1; printed kcat/Km = 166 mM^-1 s^-1.


column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180E', ATP column group; column 'Km (mM)' = 6.2; column 'kcat (s^-1)' = 919; column 'kcat/Km (mM^-1 s^-1)' = 148.

normalized_value_unit_evidence: Km: printed TABLE II cell 6.2 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 6.2 mM. kcat: printed TABLE II cell 919 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 919.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 148 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 148.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180E', ATP column group: Km = 6.2 mM; kcat = 919 s^-1; printed kcat/Km = 148 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H180D to reconstruct the assayed variant sequence.

column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180D', acetate column group; column 'Km (mM)' = 13; column 'kcat (s^-1)' = 529; column 'kcat/Km (mM^-1 s^-1)' = 40.

normalized_value_unit_evidence: Km: printed TABLE II cell 13 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 13.0 mM. kcat: printed TABLE II cell 529 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 529.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 40 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 40.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180D', acetate column group: Km = 13 mM; kcat = 529 s^-1; printed kcat/Km = 40 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H180R to reconstruct the assayed variant sequence.

column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180R', ATP column group; column 'Km (mM)' = 1.4; column 'kcat (s^-1)' = 216; column 'kcat/Km (mM^-1 s^-1)' = 159.

normalized_value_unit_evidence: Km: printed TABLE II cell 1.4 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 1.4 mM. kcat: printed TABLE II cell 216 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 216.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 159 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 159.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180R', ATP column group: Km = 1.4 mM; kcat = 216 s^-1; printed kcat/Km = 159 mM^-1 s^-1.


column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180R', acetate column group; column 'Km (mM)' = 10; column 'kcat (s^-1)' = 200; column 'kcat/Km (mM^-1 s^-1)' = 21.

normalized_value_unit_evidence: Km: printed TABLE II cell 10 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 10.0 mM. kcat: printed TABLE II cell 200 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 200.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 21 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 21.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180R', acetate column group: Km = 10 mM; kcat = 200 s^-1; printed kcat/Km = 21 mM^-1 s^-1.


organism: Escherichia coli

substrate_name: ADP

assay_conditions_summary: pH 7.5; 283.15 K; cofactor ADP

substrate: ADP


assay_conditions_summary: pH 7.5; 283.15 K; cofactor ATP


substrate_name: acetate

substrate: acetate


substrate_name: acetyl phosphate

smiles: CC(=O)OP(=O)(O)O

substrate: acetyl phosphate


substrate_name: Acetate, acetate

substrate: Acetate, acetate


column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180Q', acetate column group; column 'Km (mM)' = 14; column 'kcat (s^-1)' = 573; column 'kcat/Km (mM^-1 s^-1)' = 43.

normalized_value_unit_evidence: Km: printed TABLE II cell 14 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 14.0 mM. kcat: printed TABLE II cell 573 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 573.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 43 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 43.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180Q', acetate column group: Km = 14 mM; kcat = 573 s^-1; printed kcat/Km = 43 mM^-1 s^-1.


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H60A to reconstruct the assayed variant sequence.

column_label: TABLE I (Kinetic parameters of acetate kinase variants obtained by replacement of conserved histidines with alanine), enzyme-form row 'H60A', acetate column group; column 'Km (mM)' = 20; column 'kcat (s^-1)' = 1036; column 'kcat/Km (mM^-1 s^-1)' = 50.

normalized_value_unit_evidence: Km: printed TABLE I cell 20 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 20.0 mM. kcat: printed TABLE I cell 1036 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1036.0 s^(-1). kcat/Km: Printed TABLE I kcat/Km cell 50 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 50.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE I, enzyme-form row 'H60A', acetate column group: Km = 20 mM; kcat = 1036 s^-1; printed kcat/Km = 50 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature N7A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'N7A', ATP column group; column 'Km (mM)' = 7.0; column 'kcat (s^-1)' = 37; column 'kcat/Km' = 5.

normalized_value_unit_evidence: kcat: printed Table I cell 37 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 37.0 s^(-1). Km: printed Table I cell 7.0 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 7.0 mM. kcat/Km: printed Table I cell 5; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 5.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'N7A', ATP column group: Km = 7.0 mM; kcat = 37 s^-1; printed kcat/Km = 5 in the efficiency column, whose unit is s^-1 mM^-1.

table_label: Table I: Kinetic constants for wild-type and variants of acetate kinase from M. thermophila (J. Biol. Chem. 276, 45059-45064, 2001)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature K14R to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'K14R', ATP column group; column 'Km (mM)' = 3.62; column 'kcat (s^-1)' = 425; column 'kcat/Km' = 117.

normalized_value_unit_evidence: kcat: printed Table I cell 425 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 425.0 s^(-1). Km: printed Table I cell 3.62 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 3.62 mM. kcat/Km: printed Table I cell 117; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 117.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'K14R', ATP column group: Km = 3.62 mM; kcat = 425 s^-1; printed kcat/Km = 117 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature S12T to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'S12T', ATP column group; column 'Km (mM)' = 3.7; column 'kcat (s^-1)' = 414; column 'kcat/Km' = 112.

normalized_value_unit_evidence: kcat: printed Table I cell 414 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 414.0 s^(-1). Km: printed Table I cell 3.7 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 3.7 mM. kcat/Km: printed Table I cell 112; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 112.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'S12T', ATP column group: Km = 3.7 mM; kcat = 414 s^-1; printed kcat/Km = 112 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature D148N to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'D148N', Acetate column group; column 'Km (mM)' = 390; column 'kcat (s^-1)' = 0.34; column 'kcat/Km' = 0.0009.

normalized_value_unit_evidence: kcat: printed Table I cell 0.34 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.34 s^(-1). Km: printed Table I cell 390 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 390.0 mM. kcat/Km: printed Table I cell 0.0009; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.0009 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'D148N', Acetate column group: Km = 390 mM; kcat = 0.34 s^-1; printed kcat/Km = 0.0009 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature S10T to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'S10T', Acetate column group; column 'Km (mM)' = 266; column 'kcat (s^-1)' = 67; column 'kcat/Km' = 0.25.

normalized_value_unit_evidence: kcat: printed Table I cell 67 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 67.0 s^(-1). Km: printed Table I cell 266 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 266.0 mM. kcat/Km: printed Table I cell 0.25; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'S10T', Acetate column group: Km = 266 mM; kcat = 67 s^-1; printed kcat/Km = 0.25 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature S10A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'S10A', ATP column group; column 'Km (mM)' = 3.2; column 'kcat (s^-1)' = 23; column 'kcat/Km' = 7.

normalized_value_unit_evidence: kcat: printed Table I cell 23 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 23.0 s^(-1). Km: printed Table I cell 3.2 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 3.2 mM. kcat/Km: printed Table I cell 7; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 7.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'S10A', ATP column group: Km = 3.2 mM; kcat = 23 s^-1; printed kcat/Km = 7 in the efficiency column, whose unit is s^-1 mM^-1.


column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'D148N', ATP column group; column 'Km (mM)' = 5.2; column 'kcat (s^-1)' = 0.39; column 'kcat/Km' = 0.1.

normalized_value_unit_evidence: kcat: printed Table I cell 0.39 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.39 s^(-1). Km: printed Table I cell 5.2 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 5.2 mM. kcat/Km: printed Table I cell 0.1; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'D148N', ATP column group: Km = 5.2 mM; kcat = 0.39 s^-1; printed kcat/Km = 0.1 in the efficiency column, whose unit is s^-1 mM^-1.


column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'K14R', Acetate column group; column 'Km (mM)' = 239; column 'kcat (s^-1)' = 482; column 'kcat/Km' = 2.

normalized_value_unit_evidence: kcat: printed Table I cell 482 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 482.0 s^(-1). Km: printed Table I cell 239 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 239.0 mM. kcat/Km: printed Table I cell 2; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 2.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'K14R', Acetate column group: Km = 239 mM; kcat = 482 s^-1; printed kcat/Km = 2 in the efficiency column, whose unit is s^-1 mM^-1.


column_label: TABLE I (Kinetic parameters of acetate kinase variants obtained by replacement of conserved histidines with alanine), enzyme-form row 'H123A', ATP column group; column 'Km (mM)' = 1.5; column 'kcat (s^-1)' = 503; column 'kcat/Km (mM^-1 s^-1)' = 336.

normalized_value_unit_evidence: Km: printed TABLE I cell 1.5 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 1.5 mM. kcat: printed TABLE I cell 503 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 503.0 s^(-1). kcat/Km: Printed TABLE I kcat/Km cell 336 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 336.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE I, enzyme-form row 'H123A', ATP column group: Km = 1.5 mM; kcat = 503 s^-1; printed kcat/Km = 336 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H184A to reconstruct the assayed variant sequence.

column_label: TABLE I (Kinetic parameters of acetate kinase variants obtained by replacement of conserved histidines with alanine), enzyme-form row 'H184A', acetate column group; column 'Km (mM)' = 15; column 'kcat (s^-1)' = 435; column 'kcat/Km (mM^-1 s^-1)' = 30.

normalized_value_unit_evidence: Km: printed TABLE I cell 15 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 15.0 mM. kcat: printed TABLE I cell 435 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 435.0 s^(-1). kcat/Km: Printed TABLE I kcat/Km cell 30 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE I, enzyme-form row 'H184A', acetate column group: Km = 15 mM; kcat = 435 s^-1; printed kcat/Km = 30 mM^-1 s^-1.


column_label: TABLE I (Kinetic parameters of acetate kinase variants obtained by replacement of conserved histidines with alanine), enzyme-form row 'H184A', ATP column group; column 'Km (mM)' = 2.7; column 'kcat (s^-1)' = 528; column 'kcat/Km (mM^-1 s^-1)' = 194.

normalized_value_unit_evidence: Km: printed TABLE I cell 2.7 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 2.7 mM. kcat: printed TABLE I cell 528 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 528.0 s^(-1). kcat/Km: Printed TABLE I kcat/Km cell 194 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 194.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE I, enzyme-form row 'H184A', ATP column group: Km = 2.7 mM; kcat = 528 s^-1; printed kcat/Km = 194 mM^-1 s^-1.


column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180D', ATP column group; column 'Km (mM)' = 4.7; column 'kcat (s^-1)' = 630; column 'kcat/Km (mM^-1 s^-1)' = 135.

normalized_value_unit_evidence: Km: printed TABLE II cell 4.7 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 4.7 mM. kcat: printed TABLE II cell 630 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 630.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 135 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 135.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180D', ATP column group: Km = 4.7 mM; kcat = 630 s^-1; printed kcat/Km = 135 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature H180K to reconstruct the assayed variant sequence.

column_label: TABLE II (Kinetic parameters of the position-180 variant acetate kinases), enzyme-form row 'H180K', acetate column group; column 'Km (mM)' = 19; column 'kcat (s^-1)' = 870; column 'kcat/Km (mM^-1 s^-1)' = 46.

normalized_value_unit_evidence: Km: printed TABLE II cell 19 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 19.0 mM. kcat: printed TABLE II cell 870 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 870.0 s^(-1). kcat/Km: Printed TABLE II kcat/Km cell 46 mM^-1 s^-1; the efficiency column of this table is already in mM^-1 s^-1, which is the same unit as s^-1 mM^-1, so no unit conversion applies and the printed cell is 46.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE II, enzyme-form row 'H180K', acetate column group: Km = 19 mM; kcat = 870 s^-1; printed kcat/Km = 46 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature D148E to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'D148E', ATP column group; column 'Km (mM)' = 5.0; column 'kcat (s^-1)' = 1.46; column 'kcat/Km' = 0.3.

normalized_value_unit_evidence: kcat: printed Table I cell 1.46 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.46 s^(-1). Km: printed Table I cell 5.0 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 5.0 mM. kcat/Km: printed Table I cell 0.3; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'D148E', ATP column group: Km = 5.0 mM; kcat = 1.46 s^-1; printed kcat/Km = 0.3 in the efficiency column, whose unit is s^-1 mM^-1.


column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'S10T', ATP column group; column 'Km (mM)' = 4.3; column 'kcat (s^-1)' = 107; column 'kcat/Km' = 25.

normalized_value_unit_evidence: kcat: printed Table I cell 107 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 107.0 s^(-1). Km: printed Table I cell 4.3 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 4.3 mM. kcat/Km: printed Table I cell 25; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 25.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'S10T', ATP column group: Km = 4.3 mM; kcat = 107 s^-1; printed kcat/Km = 25 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature N7D to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'N7D', ATP column group; column 'Km (mM)' = 5; column 'kcat (s^-1)' = 2.7; column 'kcat/Km' = 0.5.

normalized_value_unit_evidence: kcat: printed Table I cell 2.7 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.7 s^(-1). Km: printed Table I cell 5 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 5.0 mM. kcat/Km: printed Table I cell 0.5; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'N7D', ATP column group: Km = 5 mM; kcat = 2.7 s^-1; printed kcat/Km = 0.5 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G331Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


substrate_name: ITP

sequence_source: UniProtKB:P38502 direct accession lookup

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

substrate: ITP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G239S to reconstruct the assayed variant sequence.


substrate_name: TTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G331A to reconstruct the assayed variant sequence.

substrate: TTP


substrate_name: UTP

substrate: UTP


organism: Methylotuvimicrobium alcaliphilum


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: propionate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

column_label: Table 1 (Kinetic constants of StAckA catalyzed reaction), steady-state block, printed ligand row 'Propionate'; column 'Km (mM)' = 11.2; column 'Vmax (umol min-1 mg-1)' = 1250; column 'kcat (s-1)' = 940; column 'kcat/Km (s-1 mM-1)' = 85; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it.

normalized_value_unit_evidence: Km: printed Table 1 cell 11.2 under the column head mM; mM is already the canonical unit, so no unit conversion applies and the value is 11.2 mM. kcat: printed Table 1 cell 940 under the column head s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 940.0 s^(-1). kcat/Km: printed Table 1 cell 85 under the column head s-1 mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 85.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 940 / 11.2 = 83.92857142857143 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, steady-state block, printed ligand row Propionate: Km = 11.2 in a column headed Km (mM); kcat = 940 in a column headed kcat (s-1); printed kcat/Km = 85 in a column headed kcat/Km (s-1 mM-1).

table_label: Table 1: Kinetic constants of StAckA catalyzed reaction (BMC Structural Biology 2012, 12:24); printed column heads: Ligand; Km (mM); Vmax (umol min-1 mg-1); kcat (s-1); kcat/Km (s-1 mM-1).

substrate: propionate


column_label: Table 1 (Kinetic constants of StAckA catalyzed reaction), steady-state block, printed ligand row 'Acetate'; column 'Km (mM)' = 1.2; column 'Vmax (umol min-1 mg-1)' = 1560; column 'kcat (s-1)' = 1180; column 'kcat/Km (s-1 mM-1)' = 985; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.2 under the column head mM; mM is already the canonical unit, so no unit conversion applies and the value is 1.2 mM. kcat: printed Table 1 cell 1180 under the column head s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1180.0 s^(-1). kcat/Km: printed Table 1 cell 985 under the column head s-1 mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 985.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 1180 / 1.2 = 983.3333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, steady-state block, printed ligand row Acetate: Km = 1.2 in a column headed Km (mM); kcat = 1180 in a column headed kcat (s-1); printed kcat/Km = 985 in a column headed kcat/Km (s-1 mM-1).


substrate_name: formate

smiles: O=CO

column_label: Table 1 (Kinetic constants of StAckA catalyzed reaction), steady-state block, printed ligand row 'Formate'; column 'Km (mM)' = 13.5; column 'Vmax (umol min-1 mg-1)' = 1180; column 'kcat (s-1)' = 880; column 'kcat/Km (s-1 mM-1)' = 68; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.5 under the column head mM; mM is already the canonical unit, so no unit conversion applies and the value is 13.5 mM. kcat: printed Table 1 cell 880 under the column head s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 880.0 s^(-1). kcat/Km: printed Table 1 cell 68 under the column head s-1 mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 68.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 880 / 13.5 = 65.18518518518519 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, steady-state block, printed ligand row Formate: Km = 13.5 in a column headed Km (mM); kcat = 880 in a column headed kcat (s-1); printed kcat/Km = 68 in a column headed kcat/Km (s-1 mM-1).

substrate: formate


column_label: Table 1 (Kinetic constants of StAckA catalyzed reaction), steady-state block, printed ligand row 'Acetyl-phosphate'; column 'Km (mM)' = 0.28; column 'Vmax (umol min-1 mg-1)' = 2350; column 'kcat (s-1)' = 1764; column 'kcat/Km (s-1 mM-1)' = 6300; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.28 under the column head mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.28 mM. kcat: printed Table 1 cell 1764 under the column head s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1764.0 s^(-1). kcat/Km: printed Table 1 cell 6300 under the column head s-1 mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 6300.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 1764 / 0.28 = 6299.999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, steady-state block, printed ligand row Acetyl-phosphate: Km = 0.28 in a column headed Km (mM); kcat = 1764 in a column headed kcat (s-1); printed kcat/Km = 6300 in a column headed kcat/Km (s-1 mM-1).


enzyme_display_name: Acetate kinase

enzyme_name_source: UniProt P38502

sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H180A after confirming H at canonical position 180; source row links accession P38502 and PMID 10958794. and applied mutation signature H180A to reconstruct the assayed variant sequence.

enzyme: Acetate kinase


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H180K after confirming H at canonical position 180; source row links accession P38502 and PMID 10958794. and applied mutation signature H180K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H90A after confirming H at canonical position 90; source row links accession P38502 and PMID 10958794. and applied mutation signature H90A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H60A after confirming H at canonical position 60; source row links accession P38502 and PMID 10958794. and applied mutation signature H60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H180N after confirming H at canonical position 180; source row links accession P38502 and PMID 10958794. and applied mutation signature H180N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H94A after confirming H at canonical position 94; source row links accession P38502 and PMID 10958794. and applied mutation signature H94A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H208A after confirming H at canonical position 208; source row links accession P38502 and PMID 10958794. and applied mutation signature H208A to reconstruct the assayed variant sequence.


sequence_source: UniProt P38502 canonical sequence reconstructed as H94A after confirming H at canonical position 94; source row links accession P38502 and PMID 10958794.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature S11T to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'S11T', ATP column group; column 'Km (mM)' = 6.8; column 'kcat (s^-1)' = 191; column 'kcat/Km' = 28.

normalized_value_unit_evidence: kcat: printed Table I cell 191 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 191.0 s^(-1). Km: printed Table I cell 6.8 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 6.8 mM. kcat/Km: printed Table I cell 28; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 28.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'S11T', ATP column group: Km = 6.8 mM; kcat = 191 s^-1; printed kcat/Km = 28 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature N211A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'N211A', Acetate column group; column 'Km (mM)' = 111; column 'kcat (s^-1)' = 1047; column 'kcat/Km' = 9.

normalized_value_unit_evidence: kcat: printed Table I cell 1047 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1047.0 s^(-1). Km: printed Table I cell 111 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 111.0 mM. kcat/Km: printed Table I cell 9; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 9.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'N211A', Acetate column group: Km = 111 mM; kcat = 1047 s^-1; printed kcat/Km = 9 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature S10A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'S10A', Acetate column group; column 'Km (mM)' = 814; column 'kcat (s^-1)' = 21; column 'kcat/Km' = 0.03.

normalized_value_unit_evidence: kcat: printed Table I cell 21 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 21.0 s^(-1). Km: printed Table I cell 814 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 814.0 mM. kcat/Km: printed Table I cell 0.03; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'S10A', Acetate column group: Km = 814 mM; kcat = 21 s^-1; printed kcat/Km = 0.03 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature D148A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'D148A', Acetate column group; column 'Km (mM)' = 170; column 'kcat (s^-1)' = 0.57; column 'kcat/Km' = 0.003.

normalized_value_unit_evidence: kcat: printed Table I cell 0.57 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.57 s^(-1). Km: printed Table I cell 170 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 170.0 mM. kcat/Km: printed Table I cell 0.003; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 0.003 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'D148A', Acetate column group: Km = 170 mM; kcat = 0.57 s^-1; printed kcat/Km = 0.003 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38502 and applied mutation signature E384A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic constants for wild-type and variants of acetate kinase from M. thermophila), enzyme-form row 'E384A', ATP column group; column 'Km (mM)' = 7.7; column 'kcat (s^-1)' = 11.4; column 'kcat/Km' = 1.5.

normalized_value_unit_evidence: kcat: printed Table I cell 11.4 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 11.4 s^(-1). Km: printed Table I cell 7.7 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 7.7 mM. kcat/Km: printed Table I cell 1.5; the efficiency column of Table I carries no unit head of its own and divides its group's s^-1 turnover column by its group's mM Michaelis-constant column, so its unit is s^-1 mM^-1, no unit conversion applies, and the printed cell is 1.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme-form row 'E384A', ATP column group: Km = 7.7 mM; kcat = 11.4 s^-1; printed kcat/Km = 1.5 in the efficiency column, whose unit is s^-1 mM^-1.


sequence_source: UniProt REST P38502 canonical sequence; G331Q reconstructed after validating the source residue at position 331.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_source: UniProt REST P38502 canonical sequence.

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


sequence_source: UniProt REST P38502 canonical sequence; N211A reconstructed after validating the source residue at position 211.


substrate_name: CTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331Q applied during review and applied mutation signature G331Q to reconstruct the assayed variant sequence.

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331A applied during review and applied mutation signature G331A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical reviewed sequence checked directly on 2026-06-01

assay_conditions_summary: pH 7; 355.15 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331Q/I332M applied during review and applied mutation signature G331Q/I332M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331Q/I332M applied during review

assay_conditions_summary: pH 5.5; 355.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S12T substitution and applied mutation signature S12T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S11A substitution and applied mutation signature S11A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S11T substitution and applied mutation signature S11T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied N7D substitution and applied mutation signature N7D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S12A substitution and applied mutation signature S12A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied D148A substitution and applied mutation signature D148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied K14A substitution and applied mutation signature K14A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S11A substitution


sequence_source: UniProtKB:P63411 direct REST lookup

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

column_label: Table 1 (Kinetic constants of StAckA catalyzed reaction), steady-state block, printed ligand row 'ADP'; column 'Km (mM)' = 0.100; column 'Vmax (umol min-1 mg-1)' = 2340; column 'kcat (s-1)' = 1750; column 'kcat/Km (s-1 mM-1)' = 17645; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.100 under the column head mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.1 mM. kcat: printed Table 1 cell 1750 under the column head s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1750.0 s^(-1). kcat/Km: printed Table 1 cell 17645 under the column head s-1 mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 17645.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 1750 / 0.100 = 17500.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, steady-state block, printed ligand row ADP: Km = 0.100 in a column headed Km (mM); kcat = 1750 in a column headed kcat (s-1); printed kcat/Km = 17645 in a column headed kcat/Km (s-1 mM-1).


organism: Shewanella sp.

sequence_source: UniProtKB:E3W769 direct REST lookup


substrate_name: GTP

sequence_source: UniProtKB P38502 canonical wild-type sequence

substrate: GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with G331Q reconstructed after confirming residue 331=G and applied mutation signature G331Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with N211T reconstructed after confirming residue 211=N and applied mutation signature N211T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with N211S reconstructed after confirming residue 211=N and applied mutation signature N211S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38502 canonical sequence with G331Q reconstructed after confirming residue 331=G


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with G331A reconstructed after confirming residue 331=G and applied mutation signature G331A to reconstruct the assayed variant sequence.


enzyme_display_name: penicillin amidase

substrate_name: Cephaloridine

sequence_source: UniProtKB reviewed canonical sequence P06875 (REST/FASTA checked 2026-06-01)

enzyme: penicillin amidase

substrate: Cephaloridine


substrate_name: p-Nitrophenyl phenylacetate

substrate: p-Nitrophenyl phenylacetate


substrate_name: Benzylpenicilloic acid

substrate: Benzylpenicilloic acid


substrate_name: ethyl 2-phenylacetate

substrate: ethyl 2-phenylacetate


substrate_name: Phenylacetylglycine

substrate: Phenylacetylglycine


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: phenylacetate 4-nitroanilide

substrate: phenylacetate 4-nitroanilide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290. and applied mutation signature F24Y with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


substrate_name: Methyl 2-phenylacetate

sequence_source: UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290.

substrate: Methyl 2-phenylacetate


substrate_name: amoxicillin

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'amoxicillin'; wild-type column group 'WT'; column 'kcat (s^-1)' = 22; column 'Km (mM)' = 1.1; column 'kcat/Km (mM^-1 s^-1)' = 20.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22 s^-1; already in s^-1, no conversion; the exported value is 22.0 s^(-1). Km: printed Table 3 cell 1.1 mM; already in mM, no conversion; the exported value is 1.1 mM. kcat/Km: printed Table 3 cell 20 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 20.0 s^(-1)*mM^(-1); the exported value is 20.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'amoxicillin', wild-type column group 'WT': kcat = 22 s^-1; Km = 1.1 mM; printed kcat/Km = 20 mM^-1 s^-1.

row_label: Table 3, substrate row 'amoxicillin', wild-type column group 'WT'

table_label: Table 3. Steady-state kinetic parameters of wild-type penicillin acylase and the bF24A mutant for the hydrolysis of various acyl donors and antibiotics.

substrate: amoxicillin


substrate_name: D-4-Hydroxyphenylglycine amide

substrate: D-4-Hydroxyphenylglycine amide


substrate_name: D-Phenylglycine amide

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'PGA (D-phenylglycine amide)'; wild-type column group 'WT'; column 'kcat (s^-1)' = 30; column 'Km (mM)' = 40; column 'kcat/Km (mM^-1 s^-1)' = 0.75.

normalized_value_unit_evidence: kcat: printed Table 3 cell 30 s^-1; already in s^-1, no conversion; the exported value is 30.0 s^(-1). Km: printed Table 3 cell 40 mM; already in mM, no conversion; the exported value is 40.0 mM. kcat/Km: printed Table 3 cell 0.75 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 0.75 s^(-1)*mM^(-1); the exported value is 0.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'PGA (D-phenylglycine amide)', wild-type column group 'WT': kcat = 30 s^-1; Km = 40 mM; printed kcat/Km = 0.75 mM^-1 s^-1.

row_label: Table 3, substrate row 'PGA (D-phenylglycine amide)', wild-type column group 'WT'

substrate: D-Phenylglycine amide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290. and applied mutation signature F24A with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


substrate_name: D-4-Hydroxyphenylglycine methyl ester

substrate: D-4-Hydroxyphenylglycine methyl ester


sequence_variant_note: Resolved canonical sequence from UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290. and applied mutation signature F57Y with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


substrate_name: Penicillin G

sequence_source: UniProtKB reviewed entry P06875 direct FASTA

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

substrate: Penicillin G


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


column_label: Table 1 (journal page 2096 (PDF page 5)); substrate row 'NIPAB (2-nitro-5-[(phenylacetyl)amino]benzoic acid)'; wild-type column group 'WT'; column 'kcat (s^-1)' = 16.2; column 'Km (mM)' = 0.015; column 'kcat/Km (mM^-1 s^-1)' = 1080. The row's fourth column 'KiPAA (mM)' = 0.05 is the product inhibition constant.

normalized_value_unit_evidence: kcat: printed Table 1 cell 16.2 s^-1; already in s^-1, no conversion; the exported value is 16.2 s^(-1). Km: printed Table 1 cell 0.015 mM; already in mM, no conversion; the exported value is 0.011 mM. kcat/Km: printed Table 1 cell 1080 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 1080.0 s^(-1)*mM^(-1); the exported value is 1472.7272727272727 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1 (journal page 2096 (PDF page 5)), substrate row 'NIPAB (2-nitro-5-[(phenylacetyl)amino]benzoic acid)', wild-type column group 'WT': kcat = 16.2 s^-1; Km = 0.015 mM; printed kcat/Km = 1080 mM^-1 s^-1.

row_label: Table 1, substrate row 'NIPAB (2-nitro-5-[(phenylacetyl)amino]benzoic acid)', wild-type column group 'WT'

table_label: Table 1. Steady-state kinetic parameters of wild-type and penicillin acylase mutants for the hydrolysis of NIPAB and Ki values for the product phenylacetic acid (PAA).


column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'PAAM (2-phenylacetamide)'; wild-type column group 'WT'; column 'kcat (s^-1)' = 50; column 'Km (mM)' = 0.20; column 'kcat/Km (mM^-1 s^-1)' = 250.

normalized_value_unit_evidence: kcat: printed Table 3 cell 50 s^-1; already in s^-1, no conversion; the exported value is 50.0 s^(-1). Km: printed Table 3 cell 0.20 mM; already in mM, no conversion; the exported value is 0.16 mM. kcat/Km: printed Table 3 cell 250 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 250.0 s^(-1)*mM^(-1); the exported value is 312.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'PAAM (2-phenylacetamide)', wild-type column group 'WT': kcat = 50 s^-1; Km = 0.20 mM; printed kcat/Km = 250 mM^-1 s^-1.

row_label: Table 3, substrate row 'PAAM (2-phenylacetamide)', wild-type column group 'WT'


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F24->A using UniProt beta chain start 290 plus PMID 11985586 betaF24 label

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


substrate_name: cephalexin

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06875 and applied mutation signature F24A with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.

column_label: Table 3 carries one Substrate column and then two enzyme blocks, WT and bF24A, each printing the three column heads k_cat (s^-1), K_m (mM) and k_cat/K_m (mM^-1 s^-1). The cited cell set is the bF24A block of substrate row Cephalexin: k_cat (s^-1) = 9.8; K_m (mM) = 2.8; k_cat/K_m (mM^-1 s^-1) = 3.48.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.8 s^-1 in the bF24A block of substrate row Cephalexin; the printed turnover column of this table is already per second, so no unit conversion applies and the paper value is 9.8 s^(-1). Km: printed Table 3 cell 2.8 under the column head K_m (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.8 mM. kcat/Km: printed Table 3 cell 3.48 under the column head k_cat/K_m (mM^-1 s^-1); the column is already per millimolar per second, so no unit conversion applies and the paper value is 3.48 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, bF24A enzyme block, substrate row Cephalexin: kcat = 9.8 s^-1; Km = 2.8 mM; printed kcat/Km = 3.48 mM^-1 s^-1.

table_label: Table 3: Steady-state kinetic parameters of wild-type penicillin acylase and the bF24A mutant for the hydrolysis of various acyl donors and antibiotics (Eur. J. Biochem. 2002, 269(8):2093-2100)

substrate: cephalexin


substrate_name: Ampicillin

substrate: Ampicillin


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F57->W using UniProt beta chain start 290 plus PMID 11985586 betaF57 label

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


sequence_source: UniProtKB:P06875 canonical sequence from direct REST lookup

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'ampicillin'; wild-type column group 'WT'; column 'kcat (s^-1)' = 30; column 'Km (mM)' = 2.5; column 'kcat/Km (mM^-1 s^-1)' = 12.

normalized_value_unit_evidence: kcat: printed Table 3 cell 30 s^-1; already in s^-1, no conversion; the exported value is 30.0 s^(-1). Km: printed Table 3 cell 2.5 mM; already in mM, no conversion; the exported value is 2.5 mM. kcat/Km: printed Table 3 cell 12 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 12.0 s^(-1)*mM^(-1); the exported value is 12.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'ampicillin', wild-type column group 'WT': kcat = 30 s^-1; Km = 2.5 mM; printed kcat/Km = 12 mM^-1 s^-1.

row_label: Table 3, substrate row 'ampicillin', wild-type column group 'WT'


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F24->W using UniProt beta chain start 290 plus PMID 11985586 betaF24 label

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as alpha F146->W using UniProt alpha chain start 27 plus PMID 11985586 alphaF146 label

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F24->L using UniProt beta chain start 290 plus PMID 11985586 betaF24 label

sequence_variant_note: Mutation signature F24L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: cefadroxil

column_label: Table 3 carries one Substrate column and then two enzyme blocks, WT and bF24A, each printing the three column heads k_cat (s^-1), K_m (mM) and k_cat/K_m (mM^-1 s^-1). The cited cell set is the bF24A block of substrate row Cefadroxil: k_cat (s^-1) = 5.2; K_m (mM) = 0.76; k_cat/K_m (mM^-1 s^-1) = 6.87.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.2 s^-1 in the bF24A block of substrate row Cefadroxil; the printed turnover column of this table is already per second, so no unit conversion applies and the paper value is 5.2 s^(-1). Km: printed Table 3 cell 0.76 under the column head K_m (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.76 mM. kcat/Km: printed Table 3 cell 6.87 under the column head k_cat/K_m (mM^-1 s^-1); the column is already per millimolar per second, so no unit conversion applies and the paper value is 6.87 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, bF24A enzyme block, substrate row Cefadroxil: kcat = 5.2 s^-1; Km = 0.76 mM; printed kcat/Km = 6.87 mM^-1 s^-1.

substrate: cefadroxil


sequence_variant_note: Resolved canonical sequence from UniProt P06875 canonical sequence plus row-specific reconstruction: beta-chain F24 maps to canonical P06875 position 313; residue F313 was replaced with A. and applied mutation signature F24A with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


sequence_source: UniProt P06875 canonical sequence; accession checked directly against UniProt on 2026-06-01.

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'cephalexin'; wild-type column group 'WT'; column 'kcat (s^-1)' = 57; column 'Km (mM)' = 1.2; column 'kcat/Km (mM^-1 s^-1)' = 47.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 57 s^-1; already in s^-1, no conversion; the exported value is 57.0 s^(-1). Km: printed Table 3 cell 1.2 mM; already in mM, no conversion; the exported value is 1.2 mM. kcat/Km: printed Table 3 cell 47.5 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 47.5 s^(-1)*mM^(-1); the exported value is 47.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'cephalexin', wild-type column group 'WT': kcat = 57 s^-1; Km = 1.2 mM; printed kcat/Km = 47.5 mM^-1 s^-1.

row_label: Table 3, substrate row 'cephalexin', wild-type column group 'WT'


sequence_source: UniProt P06875 canonical sequence plus row-specific reconstruction: beta-chain F24 maps to canonical P06875 position 313; residue F313 was replaced with A.


substrate_name: D-Phenylglycine methyl ester

substrate: D-Phenylglycine methyl ester


column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'cefadroxil'; wild-type column group 'WT'; column 'kcat (s^-1)' = 50; column 'Km (mM)' = 1; column 'kcat/Km (mM^-1 s^-1)' = 50.

normalized_value_unit_evidence: kcat: printed Table 3 cell 50 s^-1; already in s^-1, no conversion; the exported value is 50.0 s^(-1). Km: printed Table 3 cell 1 mM; already in mM, no conversion; the exported value is 1.0 mM. kcat/Km: printed Table 3 cell 50 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 50.0 s^(-1)*mM^(-1); the exported value is 50.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'cefadroxil', wild-type column group 'WT': kcat = 50 s^-1; Km = 1 mM; printed kcat/Km = 50 mM^-1 s^-1.

row_label: Table 3, substrate row 'cefadroxil', wild-type column group 'WT'


sequence_variant_note: Resolved canonical sequence from UniProt P06875 canonical sequence plus row-specific reconstruction: beta-chain F57 maps to canonical P06875 position 346; residue F346 was replaced with L. and applied mutation signature F57L with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P06875 direct REST lookup on 2026-06-01


organism: Kluyvera citrophila

sequence_source: UniProtKB:P07941 direct REST lookup on 2026-06-01


organism: Lysinibacillus sphaericus

substrate_name: Penicillin V

sequence_source: UniProtKB:P12256 direct REST lookup on 2026-06-01

substrate: Penicillin V


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12256 direct REST lookup plus T63S/S110C/N198Y reconstruction on 2026-06-01 and applied mutation signature T63S/S110C/N198Y to reconstruct the assayed variant sequence.


organism: Providencia rettgeri

sequence_source: UniProtKB:A0A2I6UI54 direct REST lookup on 2026-06-01


organism: Streptomyces lavendulae subsp. lavendulae

substrate_name: penicillin G

sequence_source: UniProtKB:Q539C0 direct REST lookup on 2026-06-01

substrate: penicillin G


substrate_name: penicillin K

substrate: penicillin K


sequence_source: UniProtKB Q539C0 direct lookup; sequence version 1.


substrate_name: penicillin F

substrate: penicillin F


substrate_name: penicillin dihydroF

substrate: penicillin dihydroF


organism: Thermus thermophilus

sequence_source: UniProtKB Q72G76 direct lookup plus PMID 23263966 mutation-coordinate reconstruction.

sequence_variant_note: Mutation signature I57F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature L24F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature L188F/L24F/I57F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S189F matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: uncultured bacterium

sequence_source: NCBI Protein ADG60270.1 via UniParc UPI0001D2CD09 cross-reference from deleted UniProtKB D6R1Q1

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Cephalexin'; column 'kcat (S-1)' = 34.2; column 'Km (uM)' = 25.5; column 'kcat/Km (uM-1 S-1)' = 1.35.

normalized_value_unit_evidence: kcat: printed Table 3 cell 34.2 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 34.2 s^(-1). Km: printed Table 3 cell 25.5 under the column head Km (uM); 25.5 / 1000 = 0.0255 mM. kcat/Km: printed Table 3 cell 1.35 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.35 x 1000 = 1350.0 s^(-1)*mM^(-1), and that printed cell is the catalytic efficiency this pass carries over as the paper's own value. Closure disclosure: dividing the two printed component cells of the same substrate row gives 34.2 / 0.0255 = 1341.1764705882356 s^-1 mM^-1, which at the two decimals this column prints would read 1.34 uM^-1 S^-1, while the efficiency cell the table prints for this substrate row stands at 1.35 uM^-1 S^-1.

raw_value_unit_evidence: Table 3, substrate row 'Cephalexin': kcat = 34.2 under the column head kcat (S-1); Km = 25.5 under the column head Km (uM); printed kcat/Km = 1.35 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Cephalexin'

table_label: Table 3: Kinetic parameters of ACPGA001 PGA (Biotechnol Lett 2014, 36, 617-625)


sequence_source: UniProtKB P06875 sequence version 2 plus chain-aware PubMed mutation mapping; PMID 11239085 names alphaF146Y; UniProt P06875 places the alpha chain at precursor residues 27-235, so alpha F146 maps to precursor residue 172, which is F in the canonical sequence.

sequence_variant_note: Mutation signature F146Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P06875 sequence version 2 plus chain-aware PubMed mutation mapping; PMID 11239085 names alphaF146L; UniProt P06875 places the alpha chain at precursor residues 27-235, so alpha F146 maps to precursor residue 172, which is F in the canonical sequence.

sequence_variant_note: Mutation signature F146L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P06875 FASTA direct lookup, sequence version 2, reviewed Swiss-Prot entry.

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


sequence_source: UniProtKB P06875 sequence version 2 plus chain-aware PubMed mutation mapping; PMID 11985586 names betaF57 substitutions; UniProt P06875 places the beta chain at precursor residues 290-846, so beta F57 maps to precursor residue 346, which is F in the canonical sequence.

sequence_variant_note: Mutation signature F57A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 3 carries one Substrate column and then two enzyme blocks, WT and bF24A, each printing the three column heads k_cat (s^-1), K_m (mM) and k_cat/K_m (mM^-1 s^-1). The cited cell set is the bF24A block of substrate row PAAM: k_cat (s^-1) = 3.9; K_m (mM) = 2; k_cat/K_m (mM^-1 s^-1) = 1.94.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 s^-1 in the bF24A block of substrate row PAAM; the printed turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.9 s^(-1). Km: printed Table 3 cell 2 under the column head K_m (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.0 mM. kcat/Km: printed Table 3 cell 1.94 under the column head k_cat/K_m (mM^-1 s^-1); the column is already per millimolar per second, so no unit conversion applies and the paper value is 1.94 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, bF24A enzyme block, substrate row PAAM: kcat = 3.9 s^-1; Km = 2 mM; printed kcat/Km = 1.94 mM^-1 s^-1.


substrate_name: cephalothin

sequence_source: NCBI Protein ADG60270.1, linked from PMID 24338159 and UniParc UPI0001D2CD09 cross-reference; UniProt D6R1Q1 itself is deleted/inactive.

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Cephalothin'; column 'kcat (S-1)' = 78.3; column 'Km (uM)' = 15.6; column 'kcat/Km (uM-1 S-1)' = 5.02.

normalized_value_unit_evidence: kcat: printed Table 3 cell 78.3 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 78.3 s^(-1). Km: printed Table 3 cell 15.6 under the column head Km (uM); 15.6 / 1000 = 0.0156 mM. kcat/Km: printed Table 3 cell 5.02 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 5.02 x 1000 = 5020.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 78.3 / 0.0156 = 5019.2307692307695 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 5.02 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Cephalothin': kcat = 78.3 under the column head kcat (S-1); Km = 15.6 under the column head Km (uM); printed kcat/Km = 5.02 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Cephalothin'

substrate: cephalothin


substrate_name: carbenicillin

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Carbenicillin'; column 'kcat (S-1)' = 63.7; column 'Km (uM)' = 51.9; column 'kcat/Km (uM-1 S-1)' = 1.23.

normalized_value_unit_evidence: kcat: printed Table 3 cell 63.7 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 63.7 s^(-1). Km: printed Table 3 cell 51.9 under the column head Km (uM); 51.9 / 1000 = 0.0519 mM. kcat/Km: printed Table 3 cell 1.23 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.23 x 1000 = 1230.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 63.7 / 0.0519 = 1227.3603082851637 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 1.23 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Carbenicillin': kcat = 63.7 under the column head kcat (S-1); Km = 51.9 under the column head Km (uM); printed kcat/Km = 1.23 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Carbenicillin'

substrate: carbenicillin


substrate_name: ampicillin

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Ampicillin'; column 'kcat (S-1)' = 49.5; column 'Km (uM)' = 94.4; column 'kcat/Km (uM-1 S-1)' = 0.52.

normalized_value_unit_evidence: kcat: printed Table 3 cell 49.5 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 49.5 s^(-1). Km: printed Table 3 cell 94.4 under the column head Km (uM); 94.4 / 1000 = 0.0944 mM. kcat/Km: printed Table 3 cell 0.52 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.52 x 1000 = 520.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 49.5 / 0.0944 = 524.3644067796611 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 0.52 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Ampicillin': kcat = 49.5 under the column head kcat (S-1); Km = 94.4 under the column head Km (uM); printed kcat/Km = 0.52 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Ampicillin'

substrate: ampicillin


column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'NIPAB'; column 'kcat (S-1)' = 58.3; column 'Km (uM)' = 8.3; column 'kcat/Km (uM-1 S-1)' = 7.02.

normalized_value_unit_evidence: kcat: printed Table 3 cell 58.3 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 58.3 s^(-1). Km: printed Table 3 cell 8.3 under the column head Km (uM); 8.3 / 1000 = 0.0083 mM. kcat/Km: printed Table 3 cell 7.02 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 7.02 x 1000 = 7020.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 58.3 / 0.0083 = 7024.096385542168 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 7.02 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'NIPAB': kcat = 58.3 under the column head kcat (S-1); Km = 8.3 under the column head Km (uM); printed kcat/Km = 7.02 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'NIPAB'


substrate_name: amoxycillin

substrate: amoxycillin


substrate_name: cephaloridine

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Cephaloridine'; column 'kcat (S-1)' = 66.9; column 'Km (uM)' = 16.4; column 'kcat/Km (uM-1 S-1)' = 4.08.

normalized_value_unit_evidence: kcat: printed Table 3 cell 66.9 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 66.9 s^(-1). Km: printed Table 3 cell 16.4 under the column head Km (uM); 16.4 / 1000 = 0.0164 mM. kcat/Km: printed Table 3 cell 4.08 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 4.08 x 1000 = 4080.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 66.9 / 0.0164 = 4079.268292682927 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 4.08 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Cephaloridine': kcat = 66.9 under the column head kcat (S-1); Km = 16.4 under the column head Km (uM); printed kcat/Km = 4.08 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Cephaloridine'

substrate: cephaloridine


column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Penicillin G'; column 'kcat (S-1)' = 64.2; column 'Km (uM)' = 4.6; column 'kcat/Km (uM-1 S-1)' = 13.96.

normalized_value_unit_evidence: kcat: printed Table 3 cell 64.2 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 64.2 s^(-1). Km: printed Table 3 cell 4.6 under the column head Km (uM); 4.6 / 1000 = 0.0046 mM. kcat/Km: printed Table 3 cell 13.96 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 13.96 x 1000 = 13960.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 64.2 / 0.0046 = 13956.521739130436 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 13.96 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Penicillin G': kcat = 64.2 under the column head kcat (S-1); Km = 4.6 under the column head Km (uM); printed kcat/Km = 13.96 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Penicillin G'


column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Penicillin V'; column 'kcat (S-1)' = 48.4; column 'Km (uM)' = 39.3; column 'kcat/Km (uM-1 S-1)' = 1.23.

normalized_value_unit_evidence: kcat: printed Table 3 cell 48.4 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 48.4 s^(-1). Km: printed Table 3 cell 39.3 under the column head Km (uM); 39.3 / 1000 = 0.0393 mM. kcat/Km: printed Table 3 cell 1.23 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.23 x 1000 = 1230.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 48.4 / 0.0393 = 1231.5521628498727 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 1.23 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Penicillin V': kcat = 48.4 under the column head kcat (S-1); Km = 39.3 under the column head Km (uM); printed kcat/Km = 1.23 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Penicillin V'


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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72G76 / EMBL AAS82314.1 / NCBI YP_005941.1 and applied mutation signature L24F/I57F with inferred residue-numbering offset +255 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q72G76 / EMBL AAS82314.1 / NCBI YP_005941.1


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72G76 / EMBL AAS82314.1 / NCBI YP_005941.1 and applied mutation signature L188F to reconstruct the assayed variant sequence.


enzyme_display_name: xylan 1,4-beta-xylosidase

organism: Enterobacter sp.

substrate_name: xylohexaose

sequence_source: UniProtKB:V5J3M5 REST FASTA checked 2026-06-01

enzyme: xylan 1,4-beta-xylosidase

substrate: xylohexaose


organism: Geobacillus stearothermophilus

substrate_name: p-Nitrophenyl-beta-D-xylopyranoside

sequence_source: UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01

substrate: p-Nitrophenyl-beta-D-xylopyranoside


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature E522A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature E335A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature E427A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature D495G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q09LZ0 REST/FASTA checked 2026-06-01; RCSB 4RHH SIFTS full sequence coverage


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q9FLG1 direct REST lookup; source row supplied Q9FLG1.


organism: Aspergillus awamori

sequence_source: UniProtKB direct lookup of source accession B5AK91 resolved to reviewed accession Q4AEG8; sequence taken from Q4AEG8.


organism: Aspergillus niger

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB unreviewed accession A0A023J5W7 direct REST lookup; source row supplied A0A023J5W7.

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl alpha-L-arabinofuranoside

substrate: 4-nitrophenyl alpha-L-arabinofuranoside


substrate_name: 4-nitrophenyl beta-D-xylopyranoside

substrate: 4-nitrophenyl beta-D-xylopyranoside


substrate_name: xylobiose

substrate: xylobiose


substrate_name: 4-nitrophenyl alpha-L-arabinopyranoside

substrate: 4-nitrophenyl alpha-L-arabinopyranoside


organism: Geobacillus thermoleovorans

sequence_source: UniProtKB direct accession lookup Q2I2N4 on 2026-06-01

column_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A, substrate row X2 (xylobiose); column 'Km (mM)' = 12.8; column 'kcat (s^-1)' = 0.065; column 'kcat/Km (mM^-1 s^-1)' = 0.0051; column 'Concentration range (mM)' = 2–96.

normalized_value_unit_evidence: Km: printed Table 1 cell 12.8 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 12.8 mM. kcat: printed Table 1 cell 0.065 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.065 s^(-1). kcat/Km: printed Table 1 cell 0.0051 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is already the canonical unit, so no unit conversion applies and the printed cell is 0.0051 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.065 / 12.8 = 0.005078125 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row X2: Km = 12.8 mM; kcat = 0.065 s^-1; printed kcat/Km = 0.0051 mM^-1 s^-1.

row_label: Table 1, substrate row X2 (xylobiose)

table_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A (Appl Biochem Biotechnol 2009, 155:304-313, journal page 307); printed column heads Substrate, Concentration range (mM), Km (mM), kcat (s^-1) and kcat/Km (mM^-1 s^-1)


column_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A, substrate row 4NPX (4-nitrophenyl-β-D-xylopyranoside); column 'Km (mM)' = 0.550; column 'kcat (s^-1)' = 0.18; column 'kcat/Km (mM^-1 s^-1)' = 0.33; column 'Concentration range (mM)' = 0.024–9.6.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.550 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 0.55 mM. kcat: printed Table 1 cell 0.18 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.18 s^(-1). kcat/Km: printed Table 1 cell 0.33 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is already the canonical unit, so no unit conversion applies and the printed cell is 0.33 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.18 / 0.550 = 0.3272727272727272 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 4NPX: Km = 0.550 mM; kcat = 0.18 s^-1; printed kcat/Km = 0.33 mM^-1 s^-1.

row_label: Table 1, substrate row 4NPX (4-nitrophenyl-β-D-xylopyranoside)


substrate_name: xylotriose

column_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A, substrate row X3 (xylotriose); column 'Km (mM)' = 5.09; column 'kcat (s^-1)' = 0.020; column 'kcat/Km (mM^-1 s^-1)' = 0.0039; column 'Concentration range (mM)' = 1–72.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.09 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 5.09 mM. kcat: printed Table 1 cell 0.020 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.02 s^(-1). kcat/Km: printed Table 1 cell 0.0039 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is already the canonical unit, so no unit conversion applies and the printed cell is 0.0039 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.020 / 5.09 = 0.003929273084479372 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row X3: Km = 5.09 mM; kcat = 0.020 s^-1; printed kcat/Km = 0.0039 mM^-1 s^-1.

row_label: Table 1, substrate row X3 (xylotriose)

substrate: xylotriose


column_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A, substrate row 4NPA (4-nitrophenyl-α-L-arabinofuranoside); column 'Km (mM)' = 0.497; column 'kcat (s^-1)' = 1.18; column 'kcat/Km (mM^-1 s^-1)' = 2.37; column 'Concentration range (mM)' = 0.048–9.6.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.497 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 0.497 mM. kcat: printed Table 1 cell 1.18 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 1.18 s^(-1). kcat/Km: printed Table 1 cell 2.37 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is already the canonical unit, so no unit conversion applies and the printed cell is 2.37 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.18 / 0.497 = 2.374245472837022 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 4NPA: Km = 0.497 mM; kcat = 1.18 s^-1; printed kcat/Km = 2.37 mM^-1 s^-1.

row_label: Table 1, substrate row 4NPA (4-nitrophenyl-α-L-arabinofuranoside)


column_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A, substrate row muX (4-methylumbelliferyl-β-D-xylopyranoside); column 'Km (mM)' = 0.366; column 'kcat (s^-1)' = 0.208; column 'kcat/Km (mM^-1 s^-1)' = 0.57; column 'Concentration range (mM)' = 0.006–12.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.366 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 0.366 mM. kcat: printed Table 1 cell 0.208 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.208 s^(-1). kcat/Km: printed Table 1 cell 0.57 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is already the canonical unit, so no unit conversion applies and the printed cell is 0.57 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.208 / 0.366 = 0.5683060109289617 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row muX: Km = 0.366 mM; kcat = 0.208 s^-1; printed kcat/Km = 0.57 mM^-1 s^-1.

row_label: Table 1, substrate row muX (4-methylumbelliferyl-β-D-xylopyranoside)


column_label: Table 1 Michaelis–Menten Kinetic parameters for substrate hydrolysis by GbtXyl43A, substrate row muA (4-methylumbelliferyl-α-L-arabinofuranoside); column 'Km (mM)' = 0.081; column 'kcat (s^-1)' = 0.233; column 'kcat/Km (mM^-1 s^-1)' = 2.88; column 'Concentration range (mM)' = 0.006–8.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.081 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 0.081 mM. kcat: printed Table 1 cell 0.233 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.233 s^(-1). kcat/Km: printed Table 1 cell 2.88 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is already the canonical unit, so no unit conversion applies and the printed cell is 2.88 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.233 / 0.081 = 2.876543209876543 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row muA: Km = 0.081 mM; kcat = 0.233 s^-1; printed kcat/Km = 2.88 mM^-1 s^-1.

row_label: Table 1, substrate row muA (4-methylumbelliferyl-α-L-arabinofuranoside)


organism: Irpex lacteus

sequence_source: UniProtKB direct accession lookup A0A2U9Q8M3 on 2026-06-01


substrate_name: 3,4-dinitrophenyl beta-D-xylopyranoside

sequence_source: UniProtKB:A0A023J5W7 direct lookup (unreviewed TrEMBL fragment; checked 2026-06-01)

substrate: 3,4-dinitrophenyl beta-D-xylopyranoside


sequence_source: UniProtKB:O00089 direct lookup (reviewed Swiss-Prot precursor; checked 2026-06-01)


organism: Bacillus thermodenitrificans

sequence_source: UniProtKB:V5N4G7 direct lookup (unreviewed TrEMBL fragment; checked 2026-06-01)


organism: Enterobacter ludwigii

substrate_name: 4-nitrophenyl beta-D-xyloside

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

substrate: 4-nitrophenyl beta-D-xyloside


sequence_source: UniProtKB:V5J3M5 direct lookup (unreviewed TrEMBL; checked 2026-06-01)


substrate_name: xylopentaose

substrate: xylopentaose


substrate_name: xylotetraose

substrate: xylotetraose


organism: Medicago sativa

sequence_source: UniProtKB:A5JTQ2 direct REST check; PMID:17615411


organism: Prevotella ruminicola

sequence_source: UniProtKB:D5EY15 direct REST check; PMID:19304844