sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature G248R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant G248R


enzyme_display_name: 3-mercaptopyruvate sulfurtransferase

organism: Rattus norvegicus

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249K with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

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

mutation_type: substitution

data_origin: experimental

enzyme: 3-mercaptopyruvate sulfurtransferase

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature R196G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: 2-Mercaptoethanol; 3-Mercaptopyruvate

kcat_over_km_display: Not reported

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

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant S249A

substrate: 2-Mercaptoethanol; 3-Mercaptopyruvate


substrate_name: 3-Mercaptopyruvate; 2-Mercaptoethanol

sequence_source: UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant S249K

substrate: 3-Mercaptopyruvate; 2-Mercaptoethanol


source_db: brenda

kcat_display: Not reported

mutation_signature: Unknown

sequence_source: UniProtKB reviewed accession P97532 FASTA, checked directly during review.

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

source: brenda


organism: Escherichia coli

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


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


organism: Bos taurus


proof_lines: in the presence of cyanide, pH 9.55, 37°C

proof_lines: determination of thiocyanate formation, 37°C, pH 9.55

proof_lines: determination of pyruvate formation, 37°C, pH 9.55


organism: Arabidopsis thaliana

substrate_name: Cyanide; 3-Mercaptopyruvate

sequence_source: UniProtKB direct accession lookup for Q24JL3; local identity cache accession_cd83b777468f62a6

proof_lines:
MST2, 30°C
MST1, 30°C

substrate: Cyanide; 3-Mercaptopyruvate


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


sequence_source: UniProtKB direct accession lookup for O64530; local identity cache accession_30cc534ada40592e


substrate_name: 3-Mercaptopyruvate; Cyanide

substrate: 3-Mercaptopyruvate; Cyanide


organism: Homo sapiens

substrate_name: glutathione

verification_status: verified

sequence_source: UniProtKB direct accession lookup for P25325; local identity cache accession_2a6c67f5ccf0d4d7 provided identity context only

column_label: Table 2 (Summary of kinetic parameters of human MST), acceptor row 'Glutathione'; column 'Km A (mM)' = 28; column 'Km 3-MP (uM)' = 20; column 'Vmax (umol min^-1 mg^-1)' = 0.61; column 'kcat (s^-1)' = 0.3; column 'kcat/Km A (mM^-1 s^-1)' = 0.01.

normalized_value_unit_evidence: Km: printed Table 2 cell 28 mM; the column head is already mM, so no unit conversion applies and the exported value is 28.0 mM. kcat: printed Table 2 cell 0.3 s^-1; the column head is already s^-1, so no unit conversion applies and the exported value is 0.3 s^(-1). kcat/Km: the exported value 0.010714285714285714 s^(-1)*mM^(-1) is the full-precision quotient of those two printed cells, 0.3 / 28. The paper's own printed efficiency cell is 0.01 mM^-1 s^-1; mM^-1 s^-1 is already the canonical s^(-1)*mM^(-1), so that cell reads 0.01 s^(-1)*mM^(-1), which is the same quotient carried to the precision printed in that column (its rounding interval is 0.005 to 0.015).

raw_value_unit_evidence: Table 2, acceptor row 'Glutathione': column 'Km A (mM)' = 28; column 'kcat (s^-1)' = 0.3; printed column 'kcat/Km A (mM^-1 s^-1)' = 0.01.

row_label: Table 2, acceptor row 'Glutathione'

table_label: Table 2: Summary of kinetic parameters of human MST (J. Biol. Chem. 2013, 288(27):20002-20013)

substrate: glutathione

status: verified


organism: Rana temporaria

proof_lines:
mitochondrial enzyme
cytosolic enzyme


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature R187G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
R187G mutant
pH 9.7, 25°C, mutant R187G


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P97532 FASTA, supported by PubMed 8910318 rat liver MST sequence context.

proof_lines:
wild-type enzyme
pH 9.7, 25°C, wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines:
R196G mutant
pH 9.7, 25°C, mutant R196G


organism: Trichomonas vaginalis

substrate_name: thiosulfate

substrate: thiosulfate


enzyme_display_name: prolyl aminopeptidase

organism: Serratia marcescens

sequence_source: UniProtKB reviewed accession O32449

enzyme: prolyl aminopeptidase


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Phanerodontia chrysosporium

substrate_name: Pro-beta-naphthylamide

sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature E198Q to reconstruct the assayed variant sequence.

substrate: Pro-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature F133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature E227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature F231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature C267A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature.


proof_lines: pH 8.0, 45°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution E227A and applied mutation signature E227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution F223A and applied mutation signature F223A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution C267A and applied mutation signature C267A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution F231A and applied mutation signature F231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution F143A and applied mutation signature F143A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C6KI04 canonical sequence; reconstructed substitution F223A


sequence_source: UniProtKB C6KI04 canonical sequence; reconstructed substitution F143A


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution E198A and applied mutation signature E198A to reconstruct the assayed variant sequence.


substrate_name: L-leucine-p-nitroanilide

source_db: uniprot

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

substrate: L-leucine-p-nitroanilide

source: uniprot


organism: Heyndrickxia coagulans

substrate_name: Pro-Ala

substrate: Pro-Ala


organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: prolyl-pNA (at 30 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7


organism: Lactobacillus helveticus

substrate_name: Pro-pNA (at 40 degrees Celsius and pH 7.5)


substrate_name: Unknown

substrate: Unknown


organism: Solanum lycopersicum


organism: Aspergillus oryzae

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

proof_lines: 50°C, pH 7.5, mutant enzyme V147A/C185V/Y393W/K415R


sequence_source: UniProtKB:W8GG09 direct accession lookup


organism: Lactiplantibacillus plantarum

sequence_source: UniProtKB:Q890D8 direct accession lookup


substrate_name: H2O; Prolyl-p-nitroanilide

sequence_source: UniProtKB:P46544 direct accession lookup; identity reuse cache source_record sequence

substrate: H2O; Prolyl-p-nitroanilide


substrate_name: Prolyl-p-nitroanilide; H2O

sequence_source: UniProtKB:P52278 direct accession lookup; identity reuse cache source_record sequence

substrate: Prolyl-p-nitroanilide; H2O


sequence_source: UniProtKB:C6KI04 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct lookup; variant reconstructed from canonical sequence and applied mutation signature E198A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C6KI04 direct lookup


organism: Rasamsonia emersonii

sequence_source: UniProtKB Q8X1C7 direct lookup


organism: Secale cereale x Triticum turgidum subsp. durum

substrate_name: Ala-beta-naphthylamide

sequence_source: UniProtKB G9J616 direct lookup

substrate: Ala-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature Y149A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature C271A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature F236A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature F139A to reconstruct the assayed variant sequence.

proof_lines:
F139A mutant enzyme
Pro-bNA, F139A mutant enzyme


organism: Aspergillus niger

sequence_source: UniProtKB:Q96VT2 direct REST lookup


sequence_source: UniProtKB:C6L823 direct REST lookup


sequence_source: UniProtKB:W8GG09 direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:W8GG09 direct REST lookup plus explicit C185V reconstruction and applied mutation signature C185V to reconstruct the assayed variant sequence.


proof_lines: 50°C, pH 7.5, mutant enzyme V147A/C185V/K415R


proof_lines: 50°C, pH 7.5, mutant enzyme V147A/Y393W/K415R


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

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


substrate_name: Leu-Gly

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

substrate: Leu-Gly


organism: Aneurinibacillus sp.

substrate_name: Pro-para-nitroanilide

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

substrate: Pro-para-nitroanilide


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


organism: Debaryomyces hansenii


organism: Grifola frondosa

substrate_name: Ala-p-nitroanilide

substrate: Ala-p-nitroanilide


organism: Lyophyllum cinerascens


organism: Penicillium camemberti

substrate_name: Pro-p-nitroanilide

substrate: Pro-p-nitroanilide


substrate_name: proline beta-naphthylamide

sequence_source: UniProtKB reviewed O32449/PIP_SERMA, literature-linked to PMID 11011150

substrate: proline beta-naphthylamide


organism: Streptomyces plicatus


organism: Triticum aestivum


organism: Priestia megaterium

substrate_name: Pro-Asp

substrate: Pro-Asp


organism: Prunus armeniaca


organism: Serratia marcescens

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed F139A from the canonical sequence and applied mutation signature F139A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed R136A from the canonical sequence and applied mutation signature R136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed E204Q from the canonical sequence and applied mutation signature E204Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed Y149A from the canonical sequence and applied mutation signature Y149A to reconstruct the assayed variant sequence.


enzyme_display_name: oleate hydratase

organism: Elizabethkingia meningoseptica

substrate_name: Oleate; H2O

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

sequence_source: UniProtKB reviewed entry C7DLJ6 / OLHYD_ELIME direct lookup; canonical protein sequence, EC 4.2.1.53, Elizabethkingia meningoseptica.

assay_conditions_summary: pH 8; 303.15 K; buffer 20 mM Tris

proof_lines: at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1400 rpm

proof_lines: at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1000 rpm

proof_lines: at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 2200 rpm, in the presence of 2.5% isopropyl alcoho

source_databases_merged: sabio_rk brenda skid

enzyme: oleate hydratase

substrate: Oleate; H2O


organism: Macrococcoides caseolyticum

substrate_name: palmitoleic acid

sequence_source: UniProtKB reviewed entry B9E972 / OLHYD_MACCJ direct lookup; canonical protein sequence, EC 4.2.1.53, Macrococcus caseolyticus strain JCSC5402 with Macrococcoides lineage context.

substrate: palmitoleic acid


organism: Macrococcus caseolyticus

substrate_name: gamma-linolenic acid

sequence_source: UniProtKB reviewed entry B9E972 / OLHYD_MACCJ direct lookup; canonical protein sequence, EC 4.2.1.53, Macrococcus caseolyticus strain JCSC5402.

smiles: CCCCC/C=C\C/C=C\C/C=C\CCCCC(=O)O

substrate: gamma-linolenic acid


substrate_name: alpha-linolenic acid

smiles: CC/C=C\C/C=C\C/C=C\CCCCCCCC(=O)O

substrate: alpha-linolenic acid


smiles: CCCCCC/C=C\CCCCCCCC(=O)O


substrate_name: myristoleic acid

smiles: CCCCC=CCCCCCCCC(=O)O

substrate: myristoleic acid


substrate_name: oleic acid

smiles: CCCCCCCC/C=C\CCCCCCCC(=O)O

substrate: oleic acid


substrate_name: linoleic acid

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linoleic acid


organism: Lysinibacillus fusiformis

substrate_name: gamma-linolenate

substrate: gamma-linolenate


organism: Stenotrophomonas maltophilia

substrate_name: oleate

substrate: oleate


substrate_name: oleate (at 30 degrees Celsius)

assay_conditions_summary: buffer Tris; cofactor FAD

proof_lines: kcat is 1.2 sec(-1). kcat is 2.6 sec(-1) with OhyA harboring two-electron-reduced FAD (PubMed:26077980). Due to the low solubility of oleate in Tris buffer, the values given in PubMed:19465645 are approximate, the real Vmax is most likely s

substrate: oleate (at 30 degrees Celsius)


organism: Macrococcus caseolyticus (strain JCSC5402)

proof_lines: kcat is 470 min(-1) with oleate as substrate. The catalytic efficiency with oleate as substrate is 3.5-fold higher than that with palmitoleate, the second favored substrate.


organism: Streptococcus pyogenes serotype M49 (strain NZ131)

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

proof_lines: kcat is 67 min(-1) and 101 min(-1) with oleate and linoleate as substrate, respectively.


organism: Paracoccus aminophilus

sequence_source: UniProtKB REST/FASTA direct lookup for S5Y0Y3


organism: Rhodococcus erythropolis

smiles: CCCCCCCC/C=C\CCCCCCCC(=O)[O-]


organism: Staphylococcus aureus

proof_lines: K0.5 value, Hill coefficient 2.2, pH 6.0, 37°C


enzyme_display_name: 4-hydroxy-2-oxovalerate aldolase

organism: Thermus thermophilus

verification_status: corrected

normalized_value_unit_evidence: kcat: printed cell 0.08 s–1 -> 0.08 s^(-1); the catalog holds 0.08 s^(-1); no unit conversion applied. Km,app: printed cell 95 μM -> 0.095 mM (1 μM = 0.001 mM); the catalog holds 0.095 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `0.08` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 0.08 x10^4 M^-1 s^-1 = 0.8 s^-1 mM^-1. The catalog stores 0.8421052631578947 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.08 / 0.095) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 0.8 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Ca2+`

table_label: Table 2 'Relative Activities of TTHB246 with Various Divalent Metal Ions' (asset `tables[1]`)

enzyme: 4-hydroxy-2-oxovalerate aldolase

status: corrected


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.38 sec(-1) with 4-hydroxy-2-oxohexanoate as substrate. kcat is 0.41 sec(-1) with 4-hydroxy-2-oxopentanoate as substrate.


organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: (4S)-4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)

assay_conditions_summary: cofactor NADH

proof_lines: The catalytic efficiency is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate, but is 10-fold lower with 4-hydroxy-2-oxoheptanoate. It is also 25-fold higher when NADH is present than the value obtained w


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: 4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)

proof_lines: The catalytic efficiency is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate. In the presence of NADH, exhibits a 2-fold increase in kcat.


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


sequence_source: UniProtKB:Q53WI0 direct accession lookup; identity reuse cache accession_234a19ae7aa140a9


normalized_value_unit_evidence: kcat: printed cell 0.57 s–1 -> 0.57 s^(-1); the catalog holds 0.57 s^(-1); no unit conversion applied. Km,app: printed cell 45 μM -> 0.045 mM (1 μM = 0.001 mM); the catalog holds 0.045 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `1.3` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 1.3 x10^4 M^-1 s^-1 = 13.0 s^-1 mM^-1. The catalog stores 12.666666666666666 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.57 / 0.045) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 13.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Mn2+`


normalized_value_unit_evidence: kcat: printed cell 0.13 s–1 -> 0.13 s^(-1); the catalog holds 0.13 s^(-1); no unit conversion applied. Km,app: printed cell 80 μM -> 0.08 mM (1 μM = 0.001 mM); the catalog holds 0.08 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `0.16` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 0.16 x10^4 M^-1 s^-1 = 1.6 s^-1 mM^-1. The catalog stores 1.625 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.13 / 0.08) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 1.6 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Mg2+`


normalized_value_unit_evidence: kcat: printed cell 1.0 s–1 -> 1.0 s^(-1); the catalog holds 1.0 s^(-1); no unit conversion applied. Km,app: printed cell 55 μM -> 0.055 mM (1 μM = 0.001 mM); the catalog holds 0.055 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `1.9` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 1.9 x10^4 M^-1 s^-1 = 19.0 s^-1 mM^-1. The catalog stores 18.181818181818183 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (1.0 / 0.055) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 19.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Co2+`


organism: Burkholderia xenovorans


organism: Burkholderia xenovorans LB400

unit: Mswedgeone


substrate_name: glycolaldehyde

smiles: O=CCO

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', BphI column group; column 'Km,app (mM)' = 124.6; column 'kcat,app (s-1)' = 0.40; column '(kcat/Km)app (M-1 s-1)' = 3.7.

normalized_value_unit_evidence: Km: printed cell 124.6 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 124.6 mM. kcat: printed cell 0.40 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 0.4 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 3.7 M^-1 s^-1 under the printed column head (kcat/Km)app (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 / 1000 = 0.0037 s^-1 mM^-1. Quotient disclosure for this cell group: 0.40 / 124.6 = 0.003210272873194222 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', BphI column group: Km,app = 124.6 mM; kcat,app = 0.40 s^-1; printed (kcat/Km)app = 3.7 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, glycolaldehyde row, BphI column group

table_label: Table 2: Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction (Biochemistry 2010, 49, 3774-3782); the HpaI column group prints Km,app (mM), kcat,app (s-1) and (kcat/Km)app in (10^3 M-1 s-1) and the BphI column group prints Km,app (mM), kcat,app (s-1) and (kcat/Km)app in (M-1 s-1)

substrate: glycolaldehyde


ki_unit: mM


organism: Paraburkholderia xenovorans

substrate_name: Butyraldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature L87A to reconstruct the assayed variant sequence.

proof_lines: aldol addition reaction with propionaldehyde, L87A mutant protein, pH 8.0, 25°C

substrate: Butyraldehyde


substrate_name: pyruvate

sequence_source: UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present

proof_lines: aldol addition reaction with propionaldehyde, wild type protein, pH 8.0, 25°C

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature L87A/L89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature R16K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature Y290F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature Y290S to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: (R,S)-glyceraldehyde

smiles: O=CC(O)CO

substrate: (R,S)-glyceraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


organism: Mycobacterium tuberculosis

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

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C

proof_lines: in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C

source_databases_merged: brenda skid


organism: Paraburkholderia xenovorans LB400

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES; cofactor NADH

proof_lines: at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate

proof_lines: in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml


normalized_value_unit_evidence: kcat: printed cell 0.79 s–1 -> 0.79 s^(-1); the catalog holds 0.79 s^(-1); no unit conversion applied. Km,app: printed cell 74 μM -> 0.074 mM (1 μM = 0.001 mM); the catalog holds 0.074 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `1.1` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 1.1 x10^4 M^-1 s^-1 = 11.0 s^-1 mM^-1. The catalog stores 10.675675675675677 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.79 / 0.074) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 11.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Ni2+`


substrate_name: propanal

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'propionaldehyde', BphI column group; column 'Km,app (mM)' = 135.9; column 'kcat,app (s-1)' = 1.79; column '(kcat/Km)app (M-1 s-1)' = 13.2.

normalized_value_unit_evidence: Km: printed cell 135.9 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 135.9 mM. kcat: printed cell 1.79 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 1.79 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 13.2 M^-1 s^-1 under the printed column head (kcat/Km)app (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13.2 / 1000 = 0.0132 s^-1 mM^-1. Quotient disclosure for this cell group: 1.79 / 135.9 = 0.013171449595290655 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'propionaldehyde', BphI column group: Km,app = 135.9 mM; kcat,app = 1.79 s^-1; printed (kcat/Km)app = 13.2 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, propionaldehyde row, BphI column group

substrate: propanal


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

column_label: Table 3 (Steady-State Kinetic Parameters of HpaI and BphI for the Aldol Addition Reaction), enzyme row 'BphI'; column 'kcat (s-1)' = 1.04; column 'KmA (mM)' = 14.8, the Michaelis constant of pyruvate (substrate A); Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 1.04 s^-1; the printed column head is kcat (s-1), so no unit conversion applies and the paper value is 1.04 s^(-1), this article printing no min^-1 kinetic cell. Km: printed cell 14.8 mM; the printed column head is KmA (mM), so no unit conversion applies and the paper value is 14.8 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.07027027027027027 s^(-1)*mM^(-1) is not a printed value; it is the quotient 1.04 / 14.8 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'BphI': kcat = 1.04 s^-1; KmA = 14.8 mM, the Michaelis constant of pyruvate (substrate A). No kcat/Km value is printed for this measurement.

row_label: Table 3, BphI row, pyruvate (substrate A) axis

table_label: Table 3: Steady-State Kinetic Parameters of HpaI and BphI for the Aldol Addition Reaction (Biochemistry 2010, 49, 3774-3782); printed columns kcat (s-1), KiA (mM), KmA (mM) and KmB (mM), with pyruvate as substrate A and acetaldehyde as substrate B


substrate_name: Acetaldehyde

smiles: CC=O

column_label: Table 3 (Steady-State Kinetic Parameters of HpaI and BphI for the Aldol Addition Reaction), enzyme row 'BphI'; column 'kcat (s-1)' = 1.04; column 'KmB (mM)' = 67.0, the Michaelis constant of acetaldehyde (substrate B); Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 1.04 s^-1; the printed column head is kcat (s-1), so no unit conversion applies and the paper value is 1.04 s^(-1), this article printing no min^-1 kinetic cell. Km: printed cell 67.0 mM; the printed column head is KmB (mM), so no unit conversion applies and the paper value is 67.0 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.015522388059701494 s^(-1)*mM^(-1) is not a printed value; it is the quotient 1.04 / 67.0 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'BphI': kcat = 1.04 s^-1; KmB = 67.0 mM, the Michaelis constant of acetaldehyde (substrate B). No kcat/Km value is printed for this measurement.

row_label: Table 3, BphI row, acetaldehyde (substrate B) axis

substrate: Acetaldehyde


substrate_name: acetaldehyde

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'acetaldehyde', HpaI column group; column 'Km,app (mM)' = 62.9; column 'kcat,app (s-1)' = 205.4; column '(kcat/Km)app (10^3 M-1 s-1)' = 3.3.

normalized_value_unit_evidence: Km: printed cell 62.9 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 62.9 mM. kcat: printed cell 205.4 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 205.4 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 3.3 x 10^3 M^-1 s^-1 under the printed column head (kcat/Km)app (10^3 M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3300.0 / 1000 = 3.3 s^-1 mM^-1. Quotient disclosure for this cell group: 205.4 / 62.9 = 3.2655007949125596 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'acetaldehyde', HpaI column group: Km,app = 62.9 mM; kcat,app = 205.4 s^-1; printed (kcat/Km)app = 3.3 x 10^3 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, acetaldehyde row, HpaI column group

substrate: acetaldehyde


smiles: CCCC=O

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'butyraldehyde', HpaI column group; column 'Km,app (mM)' = 13.4; column 'kcat,app (s-1)' = 132.5; column '(kcat/Km)app (10^3 M-1 s-1)' = 9.9.

normalized_value_unit_evidence: Km: printed cell 13.4 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 13.4 mM. kcat: printed cell 132.5 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 132.5 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 9.9 x 10^3 M^-1 s^-1 under the printed column head (kcat/Km)app (10^3 M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9900.0 / 1000 = 9.9 s^-1 mM^-1. Quotient disclosure for this cell group: 132.5 / 13.4 = 9.888059701492537 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'butyraldehyde', HpaI column group: Km,app = 13.4 mM; kcat,app = 132.5 s^-1; printed (kcat/Km)app = 9.9 x 10^3 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, butyraldehyde row, HpaI column group


column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', HpaI column group; column 'Km,app (mM)' = 33.3; column 'kcat,app (s-1)' = 175.5; column '(kcat/Km)app (10^3 M-1 s-1)' = 5.27.

normalized_value_unit_evidence: Km: printed cell 33.3 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 33.3 mM. kcat: printed cell 175.5 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 175.5 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 5.27 x 10^3 M^-1 s^-1 under the printed column head (kcat/Km)app (10^3 M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5270.0 / 1000 = 5.27 s^-1 mM^-1. Quotient disclosure for this cell group: 175.5 / 33.3 = 5.270270270270271 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', HpaI column group: Km,app = 33.3 mM; kcat,app = 175.5 s^-1; printed (kcat/Km)app = 5.27 x 10^3 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, glycolaldehyde row, HpaI column group


substrate_name: Succinic semialdehyde

smiles: O=CCCC(=O)O

substrate: Succinic semialdehyde


sequence_variant_note: Resolved canonical sequence from UniProtKB P51015 canonical sequence with direct L89A reconstruction and applied mutation signature L89A to reconstruct the assayed variant sequence.

proof_lines: aldol addition reaction with propionaldehyde, L89A mutant protein, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P51015 canonical sequence with direct H20A reconstruction and applied mutation signature H20A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P51015 canonical sequence with direct H20S reconstruction and applied mutation signature H20S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P51015 canonical sequence used as BphI identity context

proof_lines: in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C

proof_lines: in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C


enzyme_display_name: aminopeptidase B

organism: Caenorhabditis elegans

substrate_name: L-Lys-pNitroaniline

proof_lines: No activity with L-Asp-pNA, L-Glu-pNA or D-Leu-pNA.

enzyme: aminopeptidase B

substrate: L-Lys-pNitroaniline


organism: Bacillus subtilis (strain 168)

substrate_name: Arg-pNA

substrate: Arg-pNA


organism: Aspergillus niger


organism: Bos taurus

substrate_name: L-Lys-p-nitroanilide

substrate: L-Lys-p-nitroanilide


organism: Capra aegagrus

proof_lines:
free enzyme
immobilized enzyme


organism: Colwellia psychrerythraea


substrate_name: Cys-Gly

substrate: Cys-Gly


organism: Homo sapiens

substrate_name: L-Arg-beta-naphthylamide

proof_lines:
enzyme I
enzyme II

substrate: L-Arg-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F297Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y414F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y409F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y409F/Y414F to reconstruct the assayed variant sequence.


organism: Streptococcus gordonii

substrate_name: H2O; Arginine-4-nitroanilide / Arg-4-nitroanilide

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


organism: Bacillus subtilis

sequence_source: UniProtKB REST exact accession lookup: P25152


sequence_source: UniProtKB REST exact accession lookup: A2T1U6


substrate_name: H2O; Ala-p-nitroanilide

sequence_source: UniProtKB REST exact accession lookup: P09960

substrate: H2O; Ala-p-nitroanilide


substrate_name: Ala-p-nitroanilide

substrate: Ala-p-nitroanilide


substrate_name: H2O; Arg-4-methylcoumaryl-7-amide

sequence_source: UniProtKB REST exact accession lookup: Q6P179

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

substrate: H2O; Arg-4-methylcoumaryl-7-amide


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup: Q9H4A4 and applied mutation signature F297Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST exact accession lookup: Q9H4A4

proof_lines:
wild type enzyme, at pH 7.4 and 37°C
37°C, pH 7.4, wild-type enzyme


substrate_name: Met-enkephalin

substrate: Met-enkephalin


substrate_name: Lys 4-methylcoumarin 7-amide

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

substrate: Lys 4-methylcoumarin 7-amide


organism: Latilactobacillus sakei


organism: Mycosarcoma maydis


organism: Pediococcus acidilactici


organism: Rattus norvegicus


proof_lines:
wild type enzyme
pH 7.4, 37°C, wild-type


assay_conditions_summary: pH 7.4; 301.15 K; buffer complemented with 0

proof_lines:
at pH 7.4 and 28°C
recombinant Ap-B, at pH 7.4 and 25°C
Ap-B


organism: Streptococcus mitis

proof_lines:
enzyme II
enzyme I


organism: Sus scrofa

substrate_name: L-Lys-beta-naphthylamide

substrate: L-Lys-beta-naphthylamide


organism: Unknown


enzyme_display_name: dTDP-glucose 4,6-dehydratase

organism: Saccharothrix syringae

substrate_name: dTDP-alpha-D-glucose

sequence_source: UniProtKB live REST lookup for A0A5Q0HAF3

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

enzyme: dTDP-glucose 4,6-dehydratase

substrate: dTDP-alpha-D-glucose


organism: Salmonella typhimurium

substrate_name: dTDPglucose

sequence_source: UniProtKB live REST lookup for P26391

substrate: dTDPglucose


organism: Streptomyces venezuelae

substrate_name: UDP-alpha-D-glucose

sequence_source: UniProtKB live REST lookup for Q9ZGH3

proof_lines: 23°C, pH not specified in the publication

substrate: UDP-alpha-D-glucose


organism: Escherichia coli

substrate_name: dTDP-glucose

sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature T134S to reconstruct the assayed variant sequence.

substrate: dTDP-glucose


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature K164M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature Y160A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature K199R to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme K199R
pH 7.5, 37°C, mutant enzyme K199R


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature Y301F to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme Y301F
pH 7.5, 37°C, mutant enzyme Y301F


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature D135N/E136Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D135N/E136Q
pH 7.5, 37°C, mutant enzyme D135N/E136Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature E136A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme E136A
pH 7.5, 37°C, mutant enzyme E136A


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature D135N to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D135N
pH 7.5, 37°C, mutant enzyme D135N


organism: Acanthamoeba polyphaga Mimivirus

sequence_source: UniProtKB Q5UR12 direct accession lookup on 2026-06-04

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


organism: Aneurinibacillus thermoaerophilus

substrate_name: dTDP-D-glucose

sequence_source: UniProtKB Q93F85 direct accession lookup on 2026-06-04

substrate: dTDP-D-glucose


column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlB'; substrate row 'dTDP-d-glucose'; column 'Km (mM)' = 0.012 +/- 0.0016; column 'kcat (s-1)' = 1.9 +/- 0.079; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.012 mM; the column is already mM, so normalized Km = 0.012 mM. kcat: paper cell 1.9 s-1; the column is already s^(-1), so normalized kcat = 1.9 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 1.9 / 0.012 = 158.33333333333331 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlB', substrate row 'dTDP-d-glucose': Km = 0.012 +/- 0.0016 mM; kcat = 1.9 +/- 0.079 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlB', substrate row 'dTDP-d-glucose'


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus H232N reconstruction on 2026-06-04 and applied mutation signature H232N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus H232Q reconstruction on 2026-06-04 and applied mutation signature H232Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus C187S reconstruction on 2026-06-04 and applied mutation signature C187S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P27830 direct accession lookup on 2026-06-04

proof_lines:
pH 7.5, 18°C, wild-type enzyme
wild-type enzyme
pH 7.5, 37°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus N190H reconstruction on 2026-06-04 and applied mutation signature N190H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature E198Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme E198Q
pH 7.5, 37°C, mutant enzyme E198Q


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature E136Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme E136Q
pH 7.5, 37°C, mutant enzyme E136Q


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature K199M to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme K199M
pH 7.5, 37°C, mutant enzyme K199M


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature D135A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D135A
pH 7.5, 37°C, mutant enzyme D135A


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


sequence_source: Direct UniProtKB REST lookup for reviewed accession P55293.


sequence_source: Direct UniProtKB REST lookup for reviewed accession P27830.

proof_lines:
Raw SKiD Env: Temp=18°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Mycobacterium tuberculosis

sequence_source: Direct UniProtKB REST lookup for reviewed accession P9WN65.


assay_conditions_summary: cofactor NAD+


organism: Saccharopolyspora erythraea


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Streptomyces peucetius

substrate_name: NAD+

substrate: NAD+


organism: Streptomyces rimosus


organism: Streptomyces sp. C5


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


organism: Acanthamoeba polyphaga mimivirus

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

proof_lines: kcat is 0.27 sec(-1) for UDP-alpha-D-glucose (PubMed:32083779). kcat is 0.18 sec(-1) for dTDP-alpha-D-glucose (PubMed:32083779).


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Bos taurus

substrate_name: Acetyl-CoA; Acetyldithio-CoA

assay_conditions_summary: cofactor CoA

enzyme: acetyl-CoA C-acyltransferase

substrate: Acetyl-CoA; Acetyldithio-CoA


organism: Caenorhabditis elegans

substrate_name: 3-Oxooctanoyl-CoA; Coenzyme A

substrate: 3-Oxooctanoyl-CoA; Coenzyme A


organism: Candida tropicalis

substrate_name: Acetoacetyl-CoA; Coenzyme A

substrate: Acetoacetyl-CoA; Coenzyme A


substrate_name: Coenzyme A; Acetoacetyl-CoA

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant G116F

substrate: Coenzyme A; Acetoacetyl-CoA


substrate_name: Coenzyme A

assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA

substrate: Coenzyme A


organism: Helianthus annuus


organism: Homo sapiens

substrate_name: Coenzyme A; 3-Oxodecanoyl-CoA

substrate: Coenzyme A; 3-Oxodecanoyl-CoA


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme, synthesis reaction

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme, degradative reaction

substrate: acetyl-CoA


organism: Rattus norvegicus


organism: Thermobifida fusca

substrate_name: glutaryl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

substrate: glutaryl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: alpha-D-Glucose 1-phosphate

sequence_source: UniProtKB:Q9AGY4 direct accession lookup; sequence version 2; source PMID 12147463.

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'alpha-d-Glucose 1-phosphate'; column 'Km (mM)' = 0.20 +/- 0.036; column 'kcat (s-1)' = 13 +/- 1.1; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.20 mM; the column is already mM, so normalized Km = 0.20 mM. kcat: paper cell 13 s-1; the column is already s^(-1), so normalized kcat = 13 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 13 / 0.20 = 65.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'alpha-d-Glucose 1-phosphate': Km = 0.20 +/- 0.036 mM; kcat = 13 +/- 1.1 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'alpha-d-Glucose 1-phosphate'

substrate: alpha-D-Glucose 1-phosphate


substrate_name: dTTP

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'dTTP'; column 'Km (mM)' = 0.031 +/- 0.0040; column 'kcat (s-1)' = 8.9 +/- 0.24; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.031 mM; the column is already mM, so normalized Km = 0.031 mM. kcat: paper cell 8.9 s-1; the column is already s^(-1), so normalized kcat = 8.9 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 8.9 / 0.031 = 287.0967741935484 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'dTTP': Km = 0.031 +/- 0.0040 mM; kcat = 8.9 +/- 0.24 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'dTTP'

substrate: dTTP


substrate_name: diphosphate

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'Pyrophosphate'; column 'Km (mM)' = 0.055 +/- 0.0082; column 'kcat (s-1)' = 10 +/- 0.32; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.055 mM; the column is already mM, so normalized Km = 0.055 mM. kcat: paper cell 10 s-1; the column is already s^(-1), so normalized kcat = 10 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 10 / 0.055 = 181.8181818181818 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'Pyrophosphate': Km = 0.055 +/- 0.0082 mM; kcat = 10 +/- 0.32 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'Pyrophosphate'

substrate: diphosphate


substrate_name: alpha-D-Glucose 1-phosphate; dTTP

substrate: alpha-D-Glucose 1-phosphate; dTTP


enzyme_display_name: succinyl-CoA:acetate CoA-transferase

organism: Acetobacter aceti

substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed N347A variant after residue-coordinate check and applied mutation signature N347A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

enzyme: succinyl-CoA:acetate CoA-transferase

substrate: Acetyl-CoA


substrate_name: succinate

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed E435D variant after residue-coordinate check and applied mutation signature E435D to reconstruct the assayed variant sequence.

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

substrate: succinate


substrate_name: Propanoate

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed S71A variant after residue-coordinate check and applied mutation signature S71A to reconstruct the assayed variant sequence.

smiles: CCC(=O)O

substrate: Propanoate


substrate_name: succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed R228E variant after residue-coordinate check and applied mutation signature R228E to reconstruct the assayed variant sequence.

substrate: succinyl-CoA


substrate_name: Acetate

sequence_source: UniProtKB:B3EY95 canonical sequence; reconstructed S71A variant after residue-coordinate check

smiles: CC(=O)O

substrate: Acetate


substrate_name: Succinyl-CoA; Acetate

sequence_source: UniProtKB:B3EY95 canonical sequence; reconstructed E435D variant after residue-coordinate check

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant E435D AarC His6-tagged

proof_lines: mutant E435D, pH 8.0, temperature not specified in the publication

substrate: Succinyl-CoA; Acetate


sequence_source: UniProtKB:B3EY95 canonical sequence; reconstructed N347A variant after residue-coordinate check


substrate_name: dTDP-D-glucose

sequence_source: UniProtKB canonical FASTA:Q9AGY4; fetched 2026-06-04 via rest.uniprot.org

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'dTDP-d-glucose'; column 'Km (mM)' = 0.13 +/- 0.036; column 'kcat (s-1)' = 15 +/- 2.0; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.13 mM; the column is already mM, so normalized Km = 0.13 mM. kcat: paper cell 15 s-1; the column is already s^(-1), so normalized kcat = 15 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 15 / 0.13 = 115.38461538461539 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'dTDP-d-glucose': Km = 0.13 +/- 0.036 mM; kcat = 15 +/- 2.0 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'dTDP-d-glucose'

substrate: dTDP-D-glucose


substrate_name: UTP

sequence_source: UniProtKB canonical FASTA:Q9XUS5; fetched 2026-06-04 via rest.uniprot.org

substrate: UTP


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


proof_lines:
pH 7.5, 25°C
cosubstrate: UTP, pH 7.5, 25°C
cosubstrate: dTTP, pH 7.5, 25°C


sequence_source: UniProtKB canonical FASTA:P9WH13; fetched 2026-06-04 via rest.uniprot.org


proof_lines:
at pH 7.5 and 25Â°C
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5


organism: Saccharothrix syringae

sequence_source: UniProtKB:A0A5Q0HD10 REST lookup on 2026-06-04


organism: Salmonella typhimurium

substrate_name: dTDP-D-glucose; Diphosphate

sequence_source: UniProtKB:P26393 REST lookup on 2026-06-04

substrate: dTDP-D-glucose; Diphosphate


sequence_source: UniProtKB:C6K8M0 REST lookup on 2026-06-04; canonical sequence only

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


sequence_source: UniProtKB:C6K8M0 REST lookup on 2026-06-04; canonical DnmL sequence only

proof_lines: pH 7.2, 37°C, fusion protein of isoform DnmL with C-terminal sequence of isoform RmbA


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB:Q975F9 REST lookup on 2026-06-04

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


sequence_source: UniProtKB:B3EY95 REST lookup on 2026-06-04


substrate_name: Acetoacetate

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

substrate: Acetoacetate


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=N347A; RCSB 4EU3/PMID 23030530 structure anchor and applied mutation signature N347A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:B3EY95 canonical sequence; RCSB 4EU3/PMID 23030530 structure anchor


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=R228E; RCSB 4EU3/PMID 23030530 structure anchor and applied mutation signature R228E to reconstruct the assayed variant sequence.


substrate_name: Glutarate

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

substrate: Glutarate


sequence_source: Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=R228E; RCSB 4EU3/PMID 23030530 structure anchor


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=E435D; RCSB 4EU3/PMID 23030530 structure anchor and applied mutation signature E435D to reconstruct the assayed variant sequence.


substrate_name: Methylsuccinate

substrate: Methylsuccinate


sequence_source: Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=E435D; RCSB 4EU3/PMID 23030530 structure anchor


sequence_source: UniProtKB reviewed entry B3EY95 canonical FASTA, direct check on 2026-06-04.

assay_conditions_summary: pH 5; 298.15 K; cofactor CoA


substrate_name: Succinyl-CoA; Acetoacetate

substrate: Succinyl-CoA; Acetoacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry B3EY95 canonical FASTA, direct check on 2026-06-04. and applied mutation signature E435D to reconstruct the assayed variant sequence.


substrate_name: Formate

smiles: O=CO

substrate: Formate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry B3EY95 canonical FASTA, direct check on 2026-06-04. and applied mutation signature S71A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant S71A AarC His6-tagged

proof_lines: mutant S71A, pH 8.0, temperature not specified in the publication


substrate_name: D-Malate

substrate: D-Malate


substrate_name: Fumarate

substrate: Fumarate


substrate_name: Acetoacetyl-CoA; Coenzyme A

sequence_source: UniProtKB:P13437 direct accession lookup on 2026-06-04

substrate: Acetoacetyl-CoA; Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352Y


substrate_name: Coenzyme A; Acetoacetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352K

substrate: Coenzyme A; Acetoacetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352A


substrate_name: Coenzyme A; 3-Oxo-2-methylpalmitoyl-CoA

sequence_source: UniProtKB:P11915 direct accession lookup on 2026-06-04

substrate: Coenzyme A; 3-Oxo-2-methylpalmitoyl-CoA


sequence_source: UniProtKB:P21775 direct accession lookup on 2026-06-04


organism: Sus scrofa

substrate_name: Acetyldithio-CoA; Acetyl-CoA

sequence_source: UniProtKB:Q9TUF6 direct accession lookup on 2026-06-04

substrate: Acetyldithio-CoA; Acetyl-CoA


substrate_name: Acetate; Succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB REST B3EY95 canonical sequence with R228E reconstructed during review on 2026-06-04 and applied mutation signature R228E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant R228E AarC His6-tagged

proof_lines: mutant R228E, pH 8.0, temperature not specified in the publication

substrate: Acetate; Succinyl-CoA


substrate_name: succinate

sequence_source: UniProtKB REST B3EY95 canonical sequence with R228E reconstructed during review on 2026-06-04

substrate: succinate


substrate_name: succinyl-CoA

sequence_source: UniProtKB REST B3EY95 canonical sequence checked during review on 2026-06-04

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

proof_lines: pH 8.0, 30°C, His6-tagged wild-type enzyme and mutant E435D

substrate: succinyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST B3EY95 canonical sequence with N347A reconstructed during review on 2026-06-04 and applied mutation signature N347A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant N347A AarC His6-tagged

proof_lines: mutant N347A, pH 8.0, temperature not specified in the publication


substrate_name: L-Malate

substrate: L-Malate


sequence_source: UniProtKB REST B3EY95 canonical sequence with N347A reconstructed during review on 2026-06-04


substrate_name: oxaloacetate

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

substrate: oxaloacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST B3EY95 canonical sequence with S71A reconstructed during review on 2026-06-04 and applied mutation signature S71A to reconstruct the assayed variant sequence.


enzyme_display_name: trehalose-phosphatase

organism: Acinetobacter baumannii

substrate_name: alpha,alpha-trehalose 6-phosphate

sequence_source: UniProtKB:T2HRJ9 direct REST lookup on 2026-06-04; active UniProtKB unreviewed (TrEMBL) entry, organism Acinetobacter baumannii, EC 3.1.3.12.

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

enzyme: trehalose-phosphatase

substrate: alpha,alpha-trehalose 6-phosphate


organism: Arthrobacter sp.

substrate_name: trehalose 6-phosphate

sequence_source: UniProtKB:E9NR87 direct REST lookup on 2026-06-04; active UniProtKB unreviewed (TrEMBL) entry, organism Arthrobacter alpinus, EC 3.1.3.12.

substrate: trehalose 6-phosphate


proof_lines:
at pH 7.4 and 20°C
at pH 7.4 and 10°C
at pH 7.4 and 4°C


organism: Brugia malayi

sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=E386A; canonical residue E matched at 1-based position 386. and applied mutation signature E386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=N228A; canonical residue N matched at 1-based position 228. and applied mutation signature N228A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=Q332A; canonical residue Q matched at 1-based position 332. and applied mutation signature Q332A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=K334A; canonical residue K matched at 1-based position 334. and applied mutation signature K334A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=T339A; canonical residue T matched at 1-based position 339. and applied mutation signature T339A to reconstruct the assayed variant sequence.


enzyme_display_name: trehalose-6-phosphate phosphatase

sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature R337A to reconstruct the assayed variant sequence.

enzyme: trehalose-6-phosphate phosphatase


sequence_source: UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable

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

proof_lines: Ki above 10 mM, wild type enzyme, at pH 7.5 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature Q332A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature T339A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature E386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature D378A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature S329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature K334A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct lookup A8NS89


organism: Burkholderia pseudomallei

sequence_source: UniProtKB REST direct lookup Q63SB3


organism: Corynebacterium diphtheriae

sequence_source: UniProtKB REST direct lookup A0A811GD74


organism: Mycobacterium lentiflavum

sequence_source: UniProtKB REST direct lookup A0A0E4GVV3


organism: Mycobacterium triplex

sequence_source: UniProtKB REST direct lookup A0A024JUE5


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST direct lookup P9WFZ5


organism: Oryza sativa

sequence_source: UniProtKB REST direct lookup Q75WV3

assay_conditions_summary: 310.15 K; buffer 50mM Tris /HCl

proof_lines: in 50mM Tris /HCl buffer with 2mM MgCl2, at 37°C


organism: Oryza sativa Japonica Group

sequence_source: UniProtKB REST direct lookup Q9FWQ2

assay_conditions_summary: 310.15 K; buffer 50 mM Tris/HCl

proof_lines: in 50 mM Tris/HCl buffer with 2 mM MgCl2, at 37°C


enzyme_display_name: lacto-N-biosidase

organism: Bifidobacterium bifidum

substrate_name: H2O; p-Nitrophenyl lacto-N-bioside

sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature H263F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant H263F C-terminal His6-tagged

enzyme: lacto-N-biosidase

substrate: H2O; p-Nitrophenyl lacto-N-bioside


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature D320N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant D320N C-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature D320A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant D320A C-terminal His6-tagged


sequence_source: UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04.

proof_lines: wild-type, transglycosylation reaction, pH 4.5, 30°C

proof_lines: wild-type, hydrolysis reaction, pH 4.5, 30°C


substrate_name: p-Nitrophenyl lacto-N-bioside; Lactose

sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature Q190L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant Q190L

proof_lines: mutant Q190L, transglycosylation reaction, pH 4.5, 30°C

proof_lines: mutant Q190L, hydrolysis reaction, pH 4.5, 30°C

substrate: p-Nitrophenyl lacto-N-bioside; Lactose


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature H263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant H263A

proof_lines: mutant H263A, hydrolysis reaction, pH 4.5, 30°C

proof_lines: mutant H263A, transglycosylation reaction, pH 4.5, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature N259Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant N259Q

proof_lines: mutant N259Q, transglycosylation reaction, pH 4.5, 30°C

proof_lines: mutant N259Q, hydrolysis reaction, pH 4.5, 30°C


substrate_name: p-Nitrophenyl lacto-N-bioside; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature W394A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant W394A

proof_lines: mutant W394A, hydrolysis reaction, pH 4.5, 30°C

proof_lines: mutant W394A, transglycosylation reaction, pH 4.5, 30°C

substrate: p-Nitrophenyl lacto-N-bioside; H2O


organism: Escherichia coli

substrate_name: Xanthine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A847 and applied mutation signature D143A to reconstruct the assayed variant sequence.

column_label: Table 4 (Xanthine Kinetic Parameters for TGTs), body row 'htTGT(D143A)': column 'kcat (x10-6 s-1)' = 5.5; column 'KM (uM)' = 13; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.42; column 'relative KM' = 0.059; column 'relative kcat/KM' = 1.35. The number printed in parentheses beside each kinetic cell (0. 1, 1 and 0.04 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 4 cell 5.5 under the column head kcat (x10-6 s-1), so the cell is 5.5 x 10^-6 s^-1 and the value is 0.0000055 s^(-1). Km: printed Table 4 cell 13 under the column head KM (uM); 13 / 1000 = 0.013 mM. kcat/Km: printed Table 4 cell 0.42 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.42 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.42 x 10^-6 x 1000 = 0.00042 s^(-1)*mM^(-1). The exported values are kcat 0.000005 s^(-1), Km 0.013 mM and kcat_over_km 0.00038461538461538467 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'htTGT(D143A)': kcat = 5.5 in a column headed kcat (x10-6 s-1); KM = 13 in a column headed KM (uM); printed kcat/KM = 0.42 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 4, body row htTGT(D143A)

table_label: Table 4: Xanthine Kinetic Parameters for TGTs (Biochemistry 2006, 45(2):617-625). Printed column heads: enzyme; kcat (x10-6 s-1); KM (uM); kcat/KM (x10-6 s-1 uM-1); relative KM; relative kcat/KM.

substrate: Xanthine


substrate_name: tRNA guanine; Hypoxanthine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 FASTA checked directly; D143N reconstructed from the canonical D at residue 143. and applied mutation signature D143N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA-guanine transglycosylase(Enzyme) mutant htTGT(D143N)

substrate: tRNA guanine; Hypoxanthine


substrate_name: Hypoxanthine; tRNA guanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 FASTA checked directly; D143A reconstructed from the canonical D at residue 143. and applied mutation signature D143A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA-guanine transglycosylase(Enzyme) mutant htTGT(D143A)

substrate: Hypoxanthine; tRNA guanine


substrate_name: Hypoxanthine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A847 and applied mutation signature D143N to reconstruct the assayed variant sequence.

column_label: Table 3 (Hypoxanthine Kinetic Parameters for TGTs), body row 'htTGT(D143N)': column 'kcat (x10-6 s-1)' = 120; column 'KM (uM)' = 490; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.2; column 'relative KM' = 0.6; column 'relative kcat/KM' = 0.07. The number printed in parentheses beside each kinetic cell (05, 45 and 0.02 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 120 under the column head kcat (x10-6 s-1), so the cell is 120 x 10^-6 s^-1 and the value is 0.00012 s^(-1). Km: printed Table 3 cell 490 under the column head KM (uM); 490 / 1000 = 0.49 mM. kcat/Km: printed Table 3 cell 0.2 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.2 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.2 x 10^-6 x 1000 = 0.0002 s^(-1)*mM^(-1). The exported values are kcat 0.0001 s^(-1), Km 0.49 mM and kcat_over_km 0.00020408163265306123 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, body row 'htTGT(D143N)': kcat = 120 in a column headed kcat (x10-6 s-1); KM = 490 in a column headed KM (uM); printed kcat/KM = 0.2 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 3, body row htTGT(D143N)

table_label: Table 3: Hypoxanthine Kinetic Parameters for TGTs (Biochemistry 2006, 45(2):617-625). Printed column heads: enzyme; kcat (x10-6 s-1); KM (uM); kcat/KM (x10-6 s-1 uM-1); relative KM; relative kcat/KM.

substrate: Hypoxanthine


sequence_source: UniProtKB P0A847 FASTA checked directly.

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

column_label: Table 4 (Xanthine Kinetic Parameters for TGTs), body row 'htTGT(wt)': column 'kcat (x10-6 s-1)' = 69; column 'KM (uM)' = 224; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.31; column 'relative KM' = 1.0; column 'relative kcat/KM' = 1.0. The number printed in parentheses beside each kinetic cell (3, 28 and 0.04 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 4 cell 69 under the column head kcat (x10-6 s-1), so the cell is 69 x 10^-6 s^-1 and the value is 0.000069 s^(-1). Km: printed Table 4 cell 224 under the column head KM (uM); 224 / 1000 = 0.224 mM. kcat/Km: printed Table 4 cell 0.31 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.31 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.31 x 10^-6 x 1000 = 0.00031 s^(-1)*mM^(-1). The exported values are kcat 0.00007 s^(-1), Km 0.224 mM and kcat_over_km 0.00031249999999999995 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'htTGT(wt)': kcat = 69 in a column headed kcat (x10-6 s-1); KM = 224 in a column headed KM (uM); printed kcat/KM = 0.31 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 4, body row htTGT(wt)


substrate_name: tRNA queuine; Guanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 FASTA checked directly; D143S reconstructed from the canonical D at residue 143. and applied mutation signature D143S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA-guanine transglycosylase(Enzyme) mutant htTGT(D143S)

substrate: tRNA queuine; Guanine


column_label: Table 4 (Xanthine Kinetic Parameters for TGTs), body row 'htTGT(D143N)': column 'kcat (x10-6 s-1)' = 8.8; column 'KM (uM)' = 2.6; column 'kcat/KM (x10-6 s-1 uM-1)' = 3.4; column 'relative KM' = 0.012; column 'relative kcat/KM' = 10.9. The number printed in parentheses beside each kinetic cell (0.1, 0.2 and 0.3 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 4 cell 8.8 under the column head kcat (x10-6 s-1), so the cell is 8.8 x 10^-6 s^-1 and the value is 0.0000088 s^(-1). Km: printed Table 4 cell 2.6 under the column head KM (uM); 2.6 / 1000 = 0.0026 mM. kcat/Km: printed Table 4 cell 3.4 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 3.4 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.4 x 10^-6 x 1000 = 0.0034 s^(-1)*mM^(-1). The exported values are kcat 0.000009 s^(-1), Km 0.003 mM and kcat_over_km 0.003 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'htTGT(D143N)': kcat = 8.8 in a column headed kcat (x10-6 s-1); KM = 2.6 in a column headed KM (uM); printed kcat/KM = 3.4 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 4, body row htTGT(D143N)


sequence_variant_note: Resolved canonical sequence from UniProtKB:B3TLD6 direct REST lookup plus one-based W394F substitution validated on 2026-06-04 and applied mutation signature W394F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant W394F

proof_lines: mutant W394F, transglycosylation reaction, pH 4.5, 30°C

proof_lines: mutant W394F, hydrolysis reaction, pH 4.5, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:B3TLD6 direct REST lookup plus one-based H263R substitution validated on 2026-06-04 and applied mutation signature H263R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant H263R

proof_lines: mutant H263R, hydrolysis reaction, pH 4.5, 30°C

proof_lines: mutant H263R, transglycosylation reaction, pH 4.5, 30°C


sequence_source: UniProtKB:B3TLD6 direct REST lookup on 2026-06-04


organism: Bifidobacterium longum

substrate_name: lacto-N-fucopentaose I

sequence_source: UniProtKB:A0A024QYS6 direct REST lookup on 2026-06-04

substrate: lacto-N-fucopentaose I


substrate_name: lacto-N-tetraose

substrate: lacto-N-tetraose


sequence_source: UniProtKB:P0DW93 direct REST lookup on 2026-06-04


organism: Zymomonas mobilis

substrate_name: [tRNA]-guanine

sequence_source: UniProtKB:P28720 direct lookup on 2026-06-04; reviewed Swiss-Prot entry TGT_ZYMMO, Zymomonas mobilis subsp. mobilis strain ZM4, EC 2.4.2.29.

proof_lines: wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2

substrate: [tRNA]-guanine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P28720 direct lookup on 2026-06-04; reviewed Swiss-Prot entry TGT_ZYMMO, Zymomonas mobilis subsp. mobilis strain ZM4, EC 2.4.2.29. and applied mutation signature Y106F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature Y221A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12.

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

mutation_type: deletion

proof_lines: mutant enzyme DELTA59, at pH 7.5 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature D336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature S329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature Y225A to reconstruct the assayed variant sequence.


column_label: Table 3 (Hypoxanthine Kinetic Parameters for TGTs), body row 'htTGT(D143A)': column 'kcat (x10-6 s-1)' = 190; column 'KM (uM)' = 1550; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.1; column 'relative KM' = 1.9; column 'relative kcat/KM' = 0.03. The number printed in parentheses beside each kinetic cell (13, 170 and 0.02 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 190 under the column head kcat (x10-6 s-1), so the cell is 190 x 10^-6 s^-1 and the value is 0.00019 s^(-1). Km: printed Table 3 cell 1550 under the column head KM (uM); 1550 / 1000 = 1.55 mM. kcat/Km: printed Table 3 cell 0.1 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.1 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.1 x 10^-6 x 1000 = 0.0001 s^(-1)*mM^(-1). The exported values are kcat 0.0002 s^(-1), Km 1.55 mM and kcat_over_km 0.00012903225806451613 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, body row 'htTGT(D143A)': kcat = 190 in a column headed kcat (x10-6 s-1); KM = 1550 in a column headed KM (uM); printed kcat/KM = 0.1 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 3, body row htTGT(D143A)


sequence_source: UniProtKB reviewed accession P0A847, direct REST/FASTA check 2026-06-04


substrate_name: Queuine; tRNA guanine

sequence_source: UniProtKB reviewed accessions P0A847, P0A848, and P0A849, direct REST check 2026-06-04; all three have identical canonical sequence

substrate: Queuine; tRNA guanine


organism: Shigella flexneri

substrate_name: Unknown

sequence_source: UniProtKB reviewed accession Q54177, direct REST/FASTA check 2026-06-04

substrate: Unknown


substrate_name: pre-queuine 0

sequence_source: UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04

assay_conditions_summary: pH 7.3; 310.15 K; buffer 200 mM HEPES

proof_lines: competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2

proof_lines: at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates

substrate: pre-queuine 0


substrate_name: pre-queuine 1

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04 and applied mutation signature E235Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E235Q, Km less than 0.0005 mM, in 200 mM HEPES, pH 7.3, 20 mM MgCl2

substrate: pre-queuine 1


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04 and applied mutation signature K52M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04 and applied mutation signature Y330F to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct lookup for P0DW93 on 2026-06-04

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant BlLnbXc C-terminal truncated (31-625)


organism: Bifidobacterium longum subsp. Longum

sequence_source: UniProt REST direct lookup for A0A024QYS6 on 2026-06-04

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


organism: Bifidobacterium saguini

sequence_source: UniProt REST direct lookup for A0A087D8U9 on 2026-06-04

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant BsaXc C-terminal truncated (34-640)


organism: Ruminococcus lactaris

sequence_source: UniProt REST direct lookup for B5CMC4 on 2026-06-04

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant RlXc C-terminal truncated (27-607)


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Candida albicans

substrate_name: Laminaripentaose

sequence_source: UniProt REST direct lookup for P29717 on 2026-06-04

enzyme: glucan 1,3-beta-glucosidase

substrate: Laminaripentaose


substrate_name: Laminariheptaose

substrate: Laminariheptaose


substrate_name: Laminaribiose; H2O

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

sequence_source: UniProtKB:P29717 reviewed Swiss-Prot direct REST/FASTA lookup

substrate: Laminaribiose; H2O


substrate_name: Laminarihexaose

substrate: Laminarihexaose


substrate_name: Laminaritriose

substrate: Laminaritriose


substrate_name: Laminaritetraose

substrate: Laminaritetraose


substrate_name: p-Nitrophenyl-beta-D-glucoside

substrate: p-Nitrophenyl-beta-D-glucoside


substrate_name: Gentiobiose

substrate: Gentiobiose


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: Cellobiose

substrate: Cellobiose


organism: Brugia malayi

substrate_name: trehalose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB A8NS89 canonical sequence with Y225A reconstructed from PMID 24992307 Table 1/source mutation row and applied mutation signature Y225A to reconstruct the assayed variant sequence.

substrate: trehalose 6-phosphate


sequence_source: UniProtKB A8NS89 canonical reviewed Brugia malayi trehalose-phosphatase sequence


organism: Saccharomyces cerevisiae

substrate_name: trehalose 6-phosphate; H2O

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

substrate: trehalose 6-phosphate; H2O


organism: Stenotrophomonas maltophilia

substrate_name: alpha,alpha-trehalose 6-phosphate

substrate: alpha,alpha-trehalose 6-phosphate


organism: Stutzerimonas stutzeri

sequence_source: UniProtKB A0A4S2BAA8 unreviewed Stutzerimonas stutzeri trehalose 6-phosphate phosphatase sequence

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


organism: Thermoplasma acidophilum

sequence_source: UniProtKB Q9HIW7 reviewed Thermoplasma acidophilum trehalose-6-phosphate phosphatase-related protein sequence

proof_lines: in 50 mM Tris-HCl (pH 8.0), 5 mM dithiothreitol, and 20 mM MgCl2, at 50°C


organism: Thermus thermophilus

sequence_source: UniProtKB Q7WUI6 unreviewed Thermus thermophilus trehalose 6-phosphate phosphatase sequence


mutation_signature: Δ2

sequence_source: UniProtKB B3TLD6 canonical sequence retained as context only; row was not accepted as a reconstructed variant


enzyme_display_name: mitogen-activated protein kinase

organism: Homo sapiens

sequence_source: UniProtKB reviewed accession Q16539 direct lookup; primaryAccession=Q16539, organism=Homo sapiens, recommended name=Mitogen-activated protein kinase 14, EC=2.7.11.24.

enzyme: mitogen-activated protein kinase


sequence_source: UniProtKB reviewed accession P28482 direct lookup; primaryAccession=P28482, organism=Homo sapiens, recommended name=Mitogen-activated protein kinase 1, EC=2.7.11.24.

proof_lines: Ki below 0.000002 mM, potent, selective, and orally bioavailable inhibitor of ERK


organism: Mus musculus

substrate_name: ATP

sequence_source: UniProtKB reviewed accession P47811 direct lookup; primaryAccession=P47811, organism=Mus musculus, recommended name=Mitogen-activated protein kinase 14, EC=2.7.11.24.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: pH 7.0, 30°C, wild-type p38 isozyme alpha

substrate: ATP


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed accession P47811 after direct coordinate check of canonical residue 110=G and batch mutation_signature=G110A. and applied mutation signature G110A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant G110A of p38 isozyme alpha


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed accession P47811 after direct coordinate check of canonical residue 110=G and batch mutation_signature=G110D. and applied mutation signature G110D to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant G110D of p38 isozyme alpha


substrate_name: ATP; Protein

substrate: ATP; Protein


substrate_name: Protein

substrate: Protein


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


substrate_name: Cellotetraose

sequence_source: UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04

substrate: Cellotetraose


substrate_name: laminaribiose

substrate: laminaribiose


substrate_name: Gentiotriose

substrate: Gentiotriose


substrate_name: Laminarin

substrate: Laminarin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F144A with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F258W with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F144A/F258Y with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F258I with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


organism: Rhizomucor miehei

sequence_source: UniProtKB:A0A0B4RUW2 direct REST lookup, accessed 2026-06-04


substrate_name: Laminaran

substrate: Laminaran


substrate_name: laminaritriose

substrate: laminaritriose


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: uncultured bacterium

substrate_name: 4-nitrophenyl beta-L-fucoside

substrate: 4-nitrophenyl beta-L-fucoside


organism: Escherichia coli

sequence_source: UniProtKB:P17411 direct REST lookup, accessed 2026-06-04


sequence_source: UniProtKB:P11988 direct REST lookup, accessed 2026-06-04

column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPG-6-P; the Michaelis constant 2.5 comes from the printed column K_m (mM), the turnover number 7 from the printed column k_cat (1/s), and the catalytic efficiency 3.0 x 10^3 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 2.5 mM; already in mM, no unit conversion applies; the exported value is 2.5 mM. kcat: printed cell 7 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 7.0 s^(-1). kcat/Km: printed cell 3.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^3 / 1000 = 3.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 2.8 s^(-1)*mM^(-1), the quotient 7 / 2.5 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 3.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPG-6-P: Km = 2.5 mM; kcat = 7 1/s; printed kcat/Km = 3.0 x 10^3 M^-1 s^-1.


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Arabidopsis thaliana

substrate_name: pimeloyl-CoA

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

enzyme: 8-amino-7-oxononanoate synthase

substrate: pimeloyl-CoA


substrate_name: L-Alanine; 6-Carboxyhexanoyl-CoA

proof_lines: 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C

substrate: L-Alanine; 6-Carboxyhexanoyl-CoA


substrate_name: L-alanine

substrate: L-alanine


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


organism: Lysinibacillus sphaericus

substrate_name: 6-Carboxyhexanoyl-CoA; L-Alanine

substrate: 6-Carboxyhexanoyl-CoA; L-Alanine


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


organism: Lactobacillus gasseri


organism: Streptococcus pneumoniae

substrate_name: cellobiose 6-phosphate

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM NaH2PO4. The Enzymatic Activity Assays section states this

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Wild type', Cellobiose-6'P column group: column 'Km (uM)' = 1135; column 'kcat (s^-1)' = 170; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 1.5. The other three numeric cells of the same printed row belong to the pNP-beta-Glc6P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1135 uM; 1135 / 1000 = 1.135 mM. kcat: printed Table 2 cell 170 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 1.5 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 1.5 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 150.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 170.0 / 1.135 = 149.7797356828194 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', Cellobiose-6'P column group: Km = 1135 uM; kcat = 170 s^-1; printed kcat/Km = 1.5 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Wild type', the three Cellobiose-6'P cells (Km, kcat, kcat/Km x10^-1)

table_label: Table 2: Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P (J. Biol. Chem. 2013, 288(21):14949-14958)

substrate: cellobiose 6-phosphate


column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Wild type', pNP-beta-Glc6P column group: column 'Km (uM)' = 478; column 'kcat (s^-1)' = 195; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 4.1. The other three numeric cells of the same printed row belong to the Cellobiose-6'P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 478 uM; 478 / 1000 = 0.478 mM. kcat: printed Table 2 cell 195 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 4.1 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 4.1 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 410.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 195.0 / 0.478 = 407.9497907949791 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', pNP-beta-Glc6P column group: Km = 478 uM; kcat = 195 s^-1; printed kcat/Km = 4.1 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Wild type', the three pNP-beta-Glc6P cells (Km, kcat, kcat/Km x10^-1)