organism: Corynebacterium glutamicum

column_label: PMC full-text Discussion says the determined Km of 0.62 mM for D-lactate is similar to D-lactate dehydrogenases from Neisseria meningitidis and E. coli.

normalized_value_unit_evidence: Km normalized_value=0.62 normalized_unit=mM; CatLog row stores 0.61 mM.

raw_value_unit_evidence: Discussion prose reports the determined Km of 0.62 mM for D-lactate.

row_label: C. glutamicum Dld D-lactate Km sentence

table_label: PMC3022706 full-text Discussion prose


organism: Escherichia coli (strain K12)

substrate_name: ATP (in the presence of 0.2 mM dGTP)

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor ATP

data_origin: experimental

substrate: ATP (in the presence of 0.2 mM dGTP)

status: unverified

source: uniprot


substrate_name: GTP (in the presence of 0.8 mM dTTP)

substrate: GTP (in the presence of 0.8 mM dTTP)


substrate_name: UTP (in the presence of 0.4 mM ATP)

substrate: UTP (in the presence of 0.4 mM ATP)


enzyme_display_name: Quinohemoprotein alcohol dehydrogenase ADH-IIG

organism: Pseudomonas putida

substrate_name: ethanol

verification_status: verified

smiles: CCO

assay_conditions_summary: pH 8

column_label: Table 7 lists ADH IIG ethanol Km = 33.2 mM.

raw_value_unit_evidence: KM raw_value=33.2 raw_unit=mM

row_label: ADH IIG / Ethanol

table_label: PMID 7730276 Table 7

substrate: ethanol

status: verified


smiles: CC(CO)O

enzyme: Quinohemoprotein alcohol dehydrogenase ADH-IIG


substrate_name: glycerol

smiles: C(C(CO)O)O

column_label: Table 7 lists ADH IIG glycerol Km = 2.40 mM.

raw_value_unit_evidence: KM raw_value=2.40 raw_unit=mM

row_label: ADH IIG / Glycerol

substrate: glycerol


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: glucose 6-phosphate

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

assay_conditions_summary: pH 7

column_label: Figure 6C caption and Results text report the Km for glucose 6-phosphate/G6P as 100 uM.

raw_value_unit_evidence: Km raw_value=100 uM raw_unit=uM

row_label: M. tuberculosis FGD1 / glucose 6-phosphate (G6P)

table_label: JBC Figure 6C caption and Results paragraph

substrate: glucose 6-phosphate


enzyme_display_name: D-lactate dehydrogenase (quinone)

organism: Pseudomonas putida KT2440

substrate_name: coenzyme Q10

source_db: oed

kcat_over_km_origin: calculated

column_label: table label: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); row label: Fe-S d-iLDH / coenzyme Q10 electron acceptor; column label: kcat (s^-1), Fe-S d-iLDH; derived kcat/Km from Fe-S d-iLDH kcat and Km cells; Km (microM), Fe-S d-iLDH; raw value/unit and normalized value/unit preserved per metric; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with 1.0 mM D-lactate as substrate; electron acceptor ranges: MTT 0.003-0.25 mM, coenzyme Q10 0.003-0.03 mM, cytochrome c 0.003-0.10 mM.; captured paper segment: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); Fe-S d-iLDH / coenzyme Q10 electron acceptor; kcat 2.4 s^-1, kcat_over_km 585.3658536585365853658536585 s^-1 mM^-1, km 0.0041 mM.

normalized_value_unit_evidence: kcat normalized value: 2.4; normalized unit: s^-1; kcat_over_km normalized value: 585.3658536585365853658536585; normalized unit: s^-1 mM^-1; km normalized value: 0.0041; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 2.4; raw unit: s^-1; kcat_over_km raw value: 2.4 / 4.1; raw unit: s^-1 per microM; km raw value: 4.1; raw unit: microM

enzyme: D-lactate dehydrogenase (quinone)

substrate: coenzyme Q10

source: oed


enzyme_display_name: lactate-malate transhydrogenase

organism: Veillonella parvula

substrate_name: oxaloacetate

source_db: brenda

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

enzyme: lactate-malate transhydrogenase

substrate: oxaloacetate

source: brenda


substrate_name: L-malate

substrate: L-malate


substrate_name: L-lactate

substrate: L-lactate


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: D-lactate dehydrogenase (acceptor)

organism: Sulfurisphaera tokodaii

substrate_name: (R)-lactate

proof_lines: pH 8.5, 60°C, cosubstrate: 2,6-dichlorophenolindophenol

proof_lines: pH 8.5, 60°C, cosubstrate: 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide

enzyme: D-lactate dehydrogenase (acceptor)

substrate: (R)-lactate


substrate_name: CTP

proof_lines:
CTP reduction
ATP stimulation
class III ribonucleotide reductase

substrate: CTP


organism: Oryctolagus cuniculus

substrate_name: D-malate

substrate: D-malate


substrate_name: D-lactate

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

substrate: D-lactate


enzyme_display_name: pyridoxine 5-dehydrogenase

organism: Arthrobacter sp.

substrate_name: pyridoxine

enzyme: pyridoxine 5-dehydrogenase

substrate: pyridoxine


smiles: O=O


enzyme_display_name: dehydrogluconate dehydrogenase

organism: Gluconobacter oxydans

enzyme: dehydrogluconate dehydrogenase


organism: Aeropyrum pernix

assay_conditions_summary: pH 7; 333.15 K; cofactor FAD


organism: Candidatus Caldarchaeum subterraneum

proof_lines: pH 7.0, 60°C, electron acceptor: oxidized 2,6-dichlorophenolindophenol


enzyme_display_name: L-2-hydroxyglutarate dehydrogenase

organism: Indibacter alkaliphilus (strain CCUG 57479 / KCTC 22604 / LW1)

substrate_name: (S)-2-hydroxyglutarate (at pH 7.4 and 25 degrees Celsius)

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

proof_lines: kcat is 3.7 sec(-1) with DCPIP as electron acceptor (at pH 7.4 and 25 degrees Celsius).

enzyme: L-2-hydroxyglutarate dehydrogenase


organism: Thermoproteus tenax

proof_lines: 60°C, pH not specified in the publication


enzyme_display_name: glucoside 3-dehydrogenase (acceptor)

organism: Agrobacterium tumefaciens

substrate_name: D-glucose

enzyme: glucoside 3-dehydrogenase (acceptor)

substrate: D-glucose


substrate_name: sucrose

substrate: sucrose


substrate_name: cellobiose

substrate: cellobiose


substrate_name: Lactobionate

substrate: Lactobionate


substrate_name: Maltobionate

substrate: Maltobionate


organism: Pseudomonas sp.


enzyme_display_name: glycolate dehydrogenase

organism: Trichoderma harzianum

substrate_name: Nitro blue tetrazolium

enzyme: glycolate dehydrogenase

substrate: Nitro blue tetrazolium


substrate_name: glycolate

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

substrate: glycolate


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


organism: Homo sapiens


organism: Arabidopsis thaliana

substrate_name: (S)-2-hydroxyglutarate (with DCIP as acceptor molecule)

assay_conditions_summary: cofactor FAD

column_label: Downloaded OUP/PCP PDF states that kinetic parameters of A. thaliana L-2HGDH indicated KmL-2HG=0.24 +/- 0.08 mM.

raw_value_unit_evidence: Results text reports affinity constant KmL-2HG raw_value=0.24 +/- 0.08 raw_unit=mM.

row_label: Arabidopsis thaliana L-2HGDH with L-2HG

table_label: PDF Results section, L-2HGDH kinetic characterization


organism: Agaricus bisporus


substrate_name: D-cellobiose

substrate: D-cellobiose


substrate_name: D-xylose

substrate: D-xylose


organism: Chlamydomonas reinhardtii

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 30°C


substrate_name: L-lactate

km_display: Not reported

substrate: L-lactate


organism: Euglena gracilis


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: sorbose dehydrogenase

smiles: CCCO

enzyme: sorbose dehydrogenase


organism: Flavobacterium saccharophilum


substrate_name: validoxylamine A

substrate: validoxylamine A


enzyme_display_name: D-lactate dehydrogenase

organism: Anaerostipes hadrus

substrate_name: (R)-lactate (at pH 7.4 and 25 degrees Celsius)

proof_lines: kcat is 5.2 sec(-1) with DCPIP as electron acceptor (at pH 7.4 and 25 degrees Celsius).

enzyme: D-lactate dehydrogenase


organism: Thalassiosira pseudonana


substrate_name: L(+)-lactate

substrate: L(+)-lactate


substrate_name: D(-)-lactate

substrate: D(-)-lactate


enzyme_display_name: cellobiose dehydrogenase (acceptor)

organism: Termitomyces clypeatus

substrate_name: cellotriose

enzyme: cellobiose dehydrogenase (acceptor)

substrate: cellotriose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: cellopentaose

substrate: cellopentaose


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


substrate_name: ferricyanide

substrate: ferricyanide


organism: Phanerodontia chrysosporium


substrate_name: oxygen

substrate: oxygen


substrate_name: Mn(III)-malonate

substrate: Mn(III)-malonate


enzyme_display_name: UniProt A9XK88

organism: Thermothelomyces myriococcoides

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=6

enzyme: UniProt A9XK88

source: skid


organism: Humicola insolens

substrate_name: cellobiose

sequence_variant_note: Mutation signature C285Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: substitution

substrate: cellobiose


organism: Thermothelomyces fergusii

sequence_variant_note: Mutation signature C291Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: D-glucose

substrate: D-glucose


substrate_name: lactose

substrate: lactose


substrate_name: maltose

substrate: maltose


organism: Gluconobacter oxydans

substrate_name: L-sorbose

substrate: L-sorbose


enzyme_display_name: Glycolate oxidase subunit GlcD

organism: Escherichia coli (strain K12)

substrate_name: glycolate

proof_lines: Parameters measured from a partially purified enzyme from extracts of glycolate grown cells.

enzyme: Glycolate oxidase subunit GlcD

substrate: glycolate


substrate_name: D-lactate

substrate: D-lactate


enzyme_display_name: Glycolate oxidase subunit GlcE

enzyme: Glycolate oxidase subunit GlcE


enzyme_display_name: Glycolate oxidase iron-sulfur subunit

enzyme: Glycolate oxidase iron-sulfur subunit


organism: Sphingobacterium faecium

assay_conditions_summary: pH 6

column_label: PubMed abstract reports D-glucose apparent Km = 1.1 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=1.1 mM raw_unit=mM

row_label: Prose segment: D-glucose apparent Km

table_label: PubMed PMID 24585380 abstract


substrate_name: sucrose

column_label: PubMed abstract reports sucrose apparent Km = 1.7 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=1.7 mM raw_unit=mM

row_label: Prose segment: sucrose apparent Km

substrate: sucrose


substrate_name: validoxylamine A

column_label: PubMed abstract reports validoxylamine apparent Km = 2.1 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=2.1 mM raw_unit=mM

row_label: Prose segment: validoxylamine apparent Km

substrate: validoxylamine A


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

column_label: Kinetic analysis prose; row rDld / D-lactate; metric Km.

normalized_value_unit_evidence: Km=0.15 mM converted from 150 uM.

raw_value_unit_evidence: PMC94217 kinetic analysis reports a Km of 150 uM for D-lactate at 60 C.

row_label: rDld / D-lactate

table_label: Kinetic analysis prose


organism: Mycobacterium tuberculosis

substrate_name: oxidized coenzyme F420

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

substrate: oxidized coenzyme F420


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


organism: Escherichia coli

substrate_name: (R)-lactate

substrate: (R)-lactate


enzyme_display_name: alkan-1-ol dehydrogenase (acceptor)

organism: Sphingopyxis terrae

substrate_name: Tetraethylene glycol

smiles: C(COCCOCCOCCO)O

assay_conditions_summary: pH 9

proof_lines: mutant enzymes N511H and C472A, at pH 9.0, temperature not specified in the publication

enzyme: alkan-1-ol dehydrogenase (acceptor)

substrate: Tetraethylene glycol


proof_lines: mutant enzyme C382A, at pH 9.0, temperature not specified in the publication


proof_lines: mutant enzyme C379A, at pH 9.0, temperature not specified in the publication


organism: Archaeoglobus fulgidus


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCCCO


proof_lines: wild type enzyme, at pH 9.0, temperature not specified in the publication


proof_lines: mutant enzyme H467A, at pH 9.0, temperature not specified in the publication


organism: Trametes pubescens

proof_lines: pH 4.5, 30°C, electron acceptor: 2,6-dichlorophenol indophenol


substrate_name: cellopentaose

substrate: cellopentaose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: xylobiose

substrate: xylobiose


substrate_name: thiocellobiose

substrate: thiocellobiose


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


substrate_name: cytochrome c

substrate: cytochrome c


substrate_name: benzyl alkohol

substrate: benzyl alkohol


organism: Mycothermus thermophilus


substrate_name: maltose

proof_lines:
pH 7.5, 40°C
review, different references

substrate: maltose


substrate_name: cellotriose

substrate: cellotriose


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: benzoquinone

substrate: benzoquinone


organism: Trametes villosa

substrate_name: glucose

substrate: glucose


organism: Agroathelia rolfsii

substrate_name: cellobiose

proof_lines: electron acceptors methylene blue or methylene green

substrate: cellobiose


organism: Trametes hirsuta


substrate_name: DCPIP

substrate: DCPIP


proof_lines:
electron donor
at pH 4.5


proof_lines:
at pH 4.5
electron donor


organism: Neurospora crassa

substrate_name: maltotriose

proof_lines:
isoform CDH IIB, at pH 6.0 and 30°C
isoform CDH IIA, at pH 6.0 and 30°C

substrate: maltotriose


substrate_name: maltotetraose

proof_lines: recombinant enzyme, in 100 mM sodium acetate (pH 4.5), at 30°C

substrate: maltotetraose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: xylotriose

substrate: xylotriose


substrate_name: Mannopentaose

substrate: Mannopentaose


substrate_name: cellopentaose

substrate: cellopentaose


organism: Thermothelomyces myriococcoides

assay_conditions_summary: pH 6; 303.15 K; buffer 100 mM McIlvaine

proof_lines: recombinant wild type enzyme, in 100 mM McIlvaine buffer, pH 6.0, at 30°C


proof_lines: mutant enzyme N700S, in 100 mM McIlvaine buffer, pH 6.0, at 30°C


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


proof_lines: mutant enzyme 700S, in 100 mM McIlvaine buffer, pH 6.0, at 30°C


organism: Gelatoporia subvermispora

proof_lines: 2,6-dichloroindophenol as electron acceptor


substrate_name: D-glucose

substrate: D-glucose


substrate_name: ferricenium

substrate: ferricenium


organism: Ensifer sp. AS08

smiles: C(CO)O

assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M Tris-HCl

proof_lines: mutant enzyme H465A, in 0.1 M Tris-HCl buffer (pH 8.0), at 25°C


substrate_name: PEG-mono-4-nonylphenyl ether, averaging 10 ethoxy units


proof_lines: mutant enzyme N90A, in 0.1 M Tris-HCl buffer (pH 8.0), at 25°C

substrate: PEG-mono-4-nonylphenyl ether, averaging 10 ethoxy units


proof_lines: wild type enzyme, in 0.1 M Tris-HCl buffer (pH 8.0), at 25°C


organism: Arabidopsis thaliana


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: cellotriose

substrate: cellotriose


organism: Coprinopsis cinerea


substrate_name: maltose

proof_lines:
at pH 6.0 and 30°C
isoform CDH IIA, at pH 6.0 and 30°C
at pH 5.5 and 30°C

substrate: maltose


substrate_name: cytochrome c

substrate: cytochrome c


organism: Podospora anserina


substrate_name: lactose

substrate: lactose


organism: Thermothelomyces heterothallicus

proof_lines:
at 25°C
at 45°C


proof_lines:
at 25°C
at 45°C
at pH 4.5 and 25°C


substrate_name: ferricyanide

substrate: ferricyanide


protein_accession_database: NCBI Protein

sequence_source: paper_backed_accession:BAB61732.1 (PMID:11673442; polyethylene glycol dehydrogenase [Sphingopyxis terrae])

smiles: CCCCCCCO

column_label: Table 1 row 1-Heptanol lists K_m 0.4 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.4 raw_unit=mM; Vmax context cell=23.5 U/mg protein

table_label: Table 1. Substrate specificity of recombinant PEG-DH


column_label: Table 1 row 1-Hexanol lists K_m 0.5 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.5 raw_unit=mM; Vmax context cell=17.0 U/mg protein


substrate_name: benzyl alcohol

column_label: Table 1 row Benzyl alcohol lists K_m 0.6 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.6 raw_unit=mM; Vmax context cell=17.8 U/mg protein

row_label: Benzyl alcohol

substrate: benzyl alcohol


column_label: Table 1 row PEG 400 lists K_m 0.7 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.7 raw_unit=mM; Vmax context cell=10.2 U/mg protein

row_label: PEG 400


column_label: Table 1 row PEG 1000 lists K_m 1.6 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=1.6 raw_unit=mM; Vmax context cell=12.1 U/mg protein


substrate_name: tetraethylene glycol-monoethyl ether

smiles: CCOCCOCCOCCOCCO

column_label: Table 1 row TEG-monoethyl ether lists K_m 4.2 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=4.2 raw_unit=mM; Vmax context cell=6.6 U/mg protein

row_label: TEG-monoethyl ether

substrate: tetraethylene glycol-monoethyl ether


column_label: Table 1 row 1-Propanol lists K_m 6.6 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=6.6 raw_unit=mM; Vmax context cell=3.3 U/mg protein


substrate_name: Tetraethylene glycol

column_label: Table 1 row TEG lists K_m 14 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=14 raw_unit=mM; Vmax context cell=14.7 U/mg protein

row_label: TEG

substrate: Tetraethylene glycol


organism: Fungi


substrate_name: cellobiose

substrate: cellobiose


assay_conditions_summary: pH 4; 303.15 K; buffer 100 mM sodium acetate

proof_lines: in 100 mM sodium acetate buffer, pH 4.0, at 30°C

proof_lines: CDH modified plain screen printed electrodes at 0 mV, pH and temperature not specified in the publication

proof_lines: 2,6-dichloroindophenol as electron acceptor, at 40°C


substrate_name: maltotetraose

substrate: maltotetraose


proof_lines: 2,6-diclorindophenol as electron acceptor, at 40°C


organism: Trametes versicolor


substrate_name: xylobiose

substrate: xylobiose


organism: Flavobacterium sp.

substrate_name: n-Butyraldehyde

smiles: CCCC=O

substrate: n-Butyraldehyde


substrate_name: ferricytochrome c

proof_lines: in the presence of 30 mM NaCl, at pH 7.5 and 30°C

proof_lines: in the presence of 30 mM NaCl, at pH 5.5 and 30°C

proof_lines: in the presence of 30 mM CaCl2, at pH 5.5 and 30°C

substrate: ferricytochrome c


organism: Pseudomonas sp.


organism: Trametes sanguinea

proof_lines:
pH 4.5, 30°C, without polysaccharide
at pH 4.5 and 30°C


organism: Phanerochaete sordida


organism: Monilia sitophila


organism: Coniophora puteana


organism: Trametes hirsuta

substrate_name: cellopentaose

substrate: cellopentaose


organism: Agroathelia rolfsii

substrate_name: D-glucose

substrate: D-glucose


organism: Coniophora puteana (Schum ex Fr) Karsten


organism: Physcomitrium patens

proof_lines: at pH 6.0, temperature not specified in the publication


organism: Thermothelomyces myriococcoides


proof_lines:
pH 4.5, 25°C, recombinant enzyme
at pH 4.5


organism: Thermothelomyces fergusii


organism: Cerrena unicolor

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 4.5 and 30°C

proof_lines: with ferricytochrome c as cosubstrate, at pH 4.5 and 30°C


organism: Phanerodontia chrysosporium

proof_lines:
ferricyanide as electron acceptor
at pH 4.5 and 30°C
at pH 4.5 and 25°C


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

assay_conditions_summary: pH 5

proof_lines: recombinant enzyme from Pichia pastoris, with ferricytochrome c as cosubstrate, at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature H689V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1, Cellobiose oxidation block, enzyme row 'H689V'; column 'kcat (s-1)' = 0.002; column 'Km (µM)' = 31; Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.002 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.002 s^(-1). Km: printed Table 1 cell 31 µM; 31 / 1000 = 0.031 mM; the paper value is 0.031 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.06451612903225806 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.002 / 0.031 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Cellobiose oxidation block, enzyme row 'H689V': kcat = 0.002 s-1; Km = 31 µM; Table 1 prints no kcat/Km cell for this row.

table_label: Table 1: Steady-State Kinetic Parameters for rCDH and H689 Variants (Biochemistry 2003, 42(14):4049-4056)


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature H689A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1, Cellobiose oxidation block, enzyme row 'H689A'; column 'kcat (s-1)' = 0.003; column 'Km (µM)' = 21; Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.003 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.003 s^(-1). Km: printed Table 1 cell 21 µM; 21 / 1000 = 0.021 mM; the paper value is 0.021 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.14285714285714285 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.003 / 0.021 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Cellobiose oxidation block, enzyme row 'H689A': kcat = 0.003 s-1; Km = 21 µM; Table 1 prints no kcat/Km cell for this row.

status: corrected


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: pH 4.5, 23°C, mutant enzyme H689Q or mutant H689A

proof_lines: pH 4.5, 23°C, mutant enzyme H689Q or mutant enzyme H689A


proof_lines: pH 4.5, 23°C, mutant enzyme H689N or mutant H689Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732D with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732D', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 0.004; column 'Cellobiose oxidation Km (µM)' = 170; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.004 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.004 s^(-1). Km: printed Table 2 cell 170 µM; 170 / 1000 = 0.17 mM; the paper value is 0.17 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.023529411764705882 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.004 / 0.17 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732D', Cellobiose oxidation columns: cellobiose kcat = 0.004 s-1; cellobiose Km = 170 µM; Table 2 prints no kcat/Km cell for this row.

table_label: Table 2: Steady-State Kinetic Parameters for rCDH and the N732 Variant (Biochemistry 2003, 42(14):4049-4056)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature H689E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1, Cellobiose oxidation block, enzyme row 'H689E'; column 'kcat (s-1)' = 0.009; column 'Km (µM)' = 22; Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.009 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.009 s^(-1). Km: printed Table 1 cell 22 µM; 22 / 1000 = 0.022 mM; the paper value is 0.022 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.40909090909090906 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.009 / 0.022 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Cellobiose oxidation block, enzyme row 'H689E': kcat = 0.009 s-1; Km = 22 µM; Table 1 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732E', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 0.21; column 'Cellobiose oxidation Km (µM)' = 230; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.21 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.21 s^(-1). Km: printed Table 2 cell 230 µM; 230 / 1000 = 0.23 mM; the paper value is 0.23 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.9130434782608695 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.21 / 0.23 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732E', Cellobiose oxidation columns: cellobiose kcat = 0.21 s-1; cellobiose Km = 230 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732A', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 0.4; column 'Cellobiose oxidation Km (µM)' = 17; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.4 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.4 s^(-1). Km: printed Table 2 cell 17 µM; 17 / 1000 = 0.017 mM; the paper value is 0.017 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 23.52941176470588 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.4 / 0.017 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732A', Cellobiose oxidation columns: cellobiose kcat = 0.4 s-1; cellobiose Km = 17 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732Q', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 1.0; column 'Cellobiose oxidation Km (µM)' = 41; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.0 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 1.0 s^(-1). Km: printed Table 2 cell 41 µM; 41 / 1000 = 0.041 mM; the paper value is 0.041 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 24.390243902439025 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.0 / 0.041 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732Q', Cellobiose oxidation columns: cellobiose kcat = 1.0 s-1; cellobiose Km = 41 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732H with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732H', Lactose oxidation columns; column 'Lactose oxidation kcat (s-1)' = 1.7; column 'Lactose oxidation Km (µM)' = 2300; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.7 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 1.7 s^(-1). Km: printed Table 2 cell 2300 µM; 2300 / 1000 = 2.3 mM; the paper value is 2.3 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.7391304347826088 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.7 / 2.3 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732H', Lactose oxidation columns: lactose kcat = 1.7 s-1; lactose Km = 2300 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H689Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


substrate_name: FAD

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

assay_conditions_summary: pH 4.5; buffer 50 mM acetate; cofactor FAD

column_label: Table 1 row '-' / no added electron acceptor reports rate of FAD reduction 74 +/- 3 s^-1 for CDH.

raw_value_unit_evidence: kcat/rate raw_value=74 +/- 3 raw_unit=s^-1

row_label: CDH + no added electron acceptor

table_label: Table 1. Rate Constants of FAD and Heme Reduction of CDH in the Presence of Ferric Iron or MBQ

substrate: FAD


organism: Thermothielavioides terrestris

assay_conditions_summary: pH 6; 298.15 K; buffer pH 6

column_label: Table 3: Apparent kinetic constants for various electron donors with TtCDH (Biochimica et Biophysica Acta 2012, volume 1824, pages 802-812); printed column heads Substrate | Vmax (uM min^-1) | Km (uM) | kcat (s^-1) | kcat/Km (M^-1 s^-1). Table 3, substrate row Lactose; column Vmax (uM min^-1) = 0.829 ± 0.016; column Km (uM) = 23 ± 1.4 uM; column kcat (s^-1) = 1.40; column kcat/Km (M^-1 s^-1) = 6.2 x 10^4. captured primary segment: Lactose | Vmax 0.829 ± 0.016 uM min^-1 | Km 23 ± 1.4 uM | kcat 1.40 s^-1 | kcat/Km 6.2 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 23 uM (standard error ± 1.4 uM); 1 uM is 0.001 mM, so 23 / 1000 = 0.023 mM; the exported value is 0.023 mM. kcat: printed Table 3 cell 1.40 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 1.4 s^(-1); the exported value is 1.4 s^(-1). kcat/Km: printed Table 3 cell 6.2 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.2 x 10^4 / 1000 = 62.0 s^(-1)*mM^(-1); the exported value is 60.869565217391305 s^(-1)*mM^(-1), the quotient of the exported kcat 1.4 and Km 0.023.

raw_value_unit_evidence: Table 3, substrate row Lactose: Km = 23 ± 1.4 uM; kcat = 1.40 s^-1; printed kcat/Km = 6.2 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row Lactose


proof_lines: pH 4.5, electron acceptor: cytochrome c, wild-type enzyme

proof_lines: pH 4.5, 23°C, recombinant wild-type enzyme


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M685Y with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


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


proof_lines: pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol


proof_lines:
pH 4.5, 30°C
in presence of 0.24 mM O2
in absence of O2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M65H with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 4.5, electron acceptor: cytochrome c, mutant enzyme M65H

proof_lines: pH 4.5, electron acceptor: 2,6-dichlorophenol indophenol, mutant enzyme M65H


substrate_name: 2,6-dichlorophenol indophenol

proof_lines: pH 4.5, reaction with cellobiose, mutant enzyme M65H

substrate: 2,6-dichlorophenol indophenol


proof_lines: pH 4.5, reaction with cellobiose, wild-type enzyme


organism: Schizophyllum commune

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


substrate_name: cellotriose

substrate: cellotriose


substrate_name: cellotetraose

substrate: cellotetraose


organism: Dichomera saubinetii

assay_conditions_summary: pH 5; 303.15 K; buffer McIlvaine

column_label: Table 3 row Ds CDH IIA; cellobiose lists K_m 125 uM, kcat 27.8 s^-1, and kcat/K_m 2.22 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.125 normalized_unit=mM; kcat normalized_value=27.8 normalized_unit=s^-1; kcat/Km normalized_value=222.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=125 raw_unit=uM; kcat raw_value=27.8 raw_unit=s^-1; kcat/Km raw_value=2.22 x 10^5 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; cellobiose

table_label: Table 3. Steady-state kinetic constants for selected CDHs with carbohydrate electron donors


column_label: Table 3 row Ds CDH IIA; D-glucose lists K_m 79000 uM, kcat 23.6 s^-1, and kcat/K_m 300 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=79 normalized_unit=mM; kcat normalized_value=23.6 normalized_unit=s^-1; kcat/Km normalized_value=0.3 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=79000 raw_unit=uM; kcat raw_value=23.6 raw_unit=s^-1; kcat/Km raw_value=300 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; D-glucose


column_label: Table 3 row Ds CDH IIA; lactose lists K_m 215 uM, kcat 28.9 s^-1, and kcat/K_m 1.34 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.215 normalized_unit=mM; kcat normalized_value=28.9 normalized_unit=s^-1; kcat/Km normalized_value=134.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=215 raw_unit=uM; kcat raw_value=28.9 raw_unit=s^-1; kcat/Km raw_value=1.34 x 10^5 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; lactose


substrate_name: maltose

column_label: Table 3 row Ds CDH IIA; maltose lists K_m 8000 uM, kcat 1.38 s^-1, and kcat/K_m 175 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=8 normalized_unit=mM; kcat normalized_value=1.38 normalized_unit=s^-1; kcat/Km normalized_value=0.175 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=8000 raw_unit=uM; kcat raw_value=1.38 raw_unit=s^-1; kcat/Km raw_value=175 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; maltose

substrate: maltose


organism: Amesia atrobrunnea

assay_conditions_summary: pH 6; 303.15 K; buffer McIlvaine

column_label: Table 3 row Ca CDH IIA; cellobiose lists K_m 72 uM, kcat 20.1 s^-1, and kcat/K_m 2.79 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.072 normalized_unit=mM; kcat normalized_value=20.1 normalized_unit=s^-1; kcat/Km normalized_value=279.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=72 raw_unit=uM; kcat raw_value=20.1 raw_unit=s^-1; kcat/Km raw_value=2.79 x 10^5 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; cellobiose


column_label: Table 3 row Ca CDH IIA; D-glucose lists K_m 87000 uM, kcat 16.8 s^-1, and kcat/K_m 195 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=87 normalized_unit=mM; kcat normalized_value=16.8 normalized_unit=s^-1; kcat/Km normalized_value=0.195 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=87000 raw_unit=uM; kcat raw_value=16.8 raw_unit=s^-1; kcat/Km raw_value=195 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; D-glucose


substrate_name: lactose

column_label: Table 3 row Ca CDH IIA; lactose lists K_m 217 uM, kcat 33.7 s^-1, and kcat/K_m 1.55 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.217 normalized_unit=mM; kcat normalized_value=33.7 normalized_unit=s^-1; kcat/Km normalized_value=155.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=217 raw_unit=uM; kcat raw_value=33.7 raw_unit=s^-1; kcat/Km raw_value=1.55 x 10^5 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; lactose

substrate: lactose


column_label: Table 3 row Ca CDH IIA; maltose lists K_m 15500 uM, kcat 4.0 s^-1, and kcat/K_m 260 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=15.5 normalized_unit=mM; kcat normalized_value=4.0 normalized_unit=s^-1; kcat/Km normalized_value=0.26 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=15500 raw_unit=uM; kcat raw_value=4.0 raw_unit=s^-1; kcat/Km raw_value=260 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; maltose


assay_conditions_summary: pH 6; buffer 50 mM MES

column_label: Primary PDF page 10 (journal page 811), Table 3, Lactose row, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km=0.023 mM; kcat=1.40 s^-1; kcat/Km=62 s^-1 mM^-1. All exported values match the one printed row.

row_label: Lactose

table_label: Table 3. Apparent kinetic constants for various electron donors with TtCDH


column_label: Primary PDF page 10 (journal page 811), Table 3, Cellobiose row, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km=0.0039 mM; kcat=1.23 s^-1; kcat/Km=320 s^-1 mM^-1. All exported values match the one printed row.

row_label: Cellobiose


substrate_name: D-xylose

assay_conditions_summary: pH 6; 298.15 K; buffer 50 mM MES

column_label: Table 3: Apparent kinetic constants for various electron donors with TtCDH (Biochimica et Biophysica Acta 2012, volume 1824, pages 802-812); printed column heads Substrate | Vmax (uM min^-1) | Km (uM) | kcat (s^-1) | kcat/Km (M^-1 s^-1). Table 3, substrate row Xylose; column Vmax (uM min^-1) = 0.989 ± 0.021; column Km (uM) = 1.0 x 10^6 uM; column kcat (s^-1) = 0.33; column kcat/Km (M^-1 s^-1) = 0.33. captured primary segment: Xylose | Vmax 0.989 ± 0.021 uM min^-1 | Km 1.0 x 10^6 uM | kcat 0.33 s^-1 | kcat/Km 0.33 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 1.0 x 10^6 uM; 1 uM is 0.001 mM, so 1.0 x 10^6 / 1000 = 1000.0 mM; the exported value is 1000.0 mM. kcat: printed Table 3 cell 0.33 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 0.33 s^(-1); the exported value is 0.33 s^(-1). kcat/Km: printed Table 3 cell 0.33 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.33 / 1000 = 0.00033 s^(-1)*mM^(-1); the exported value is 0.00033 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Xylose: Km = 1.0 x 10^6 uM; kcat = 0.33 s^-1; printed kcat/Km = 0.33 M^-1 s^-1.

row_label: Table 3, substrate row Xylose

substrate: D-xylose


column_label: Primary PDF page 10 (journal page 811), Table 3, Glucose row, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km=54 mM; kcat=1.01 s^-1; printed kcat/Km=0.019 s^-1 mM^-1. The exported 0.018703703703703705 is the derived 1.01/54 quotient, not the explicit printed ratio.

row_label: Glucose


column_label: Table 3: Apparent kinetic constants for various electron donors with TtCDH (Biochimica et Biophysica Acta 2012, volume 1824, pages 802-812); printed column heads Substrate | Vmax (uM min^-1) | Km (uM) | kcat (s^-1) | kcat/Km (M^-1 s^-1). Table 3, substrate row Cellotetraose; column Vmax (uM min^-1) = 0.364 ± 0.003; column Km (uM) = 5.6 ± 0.2 uM; column kcat (s^-1) = 1.23; column kcat/Km (M^-1 s^-1) = 2.2 x 10^5. captured primary segment: Cellotetraose | Vmax 0.364 ± 0.003 uM min^-1 | Km 5.6 ± 0.2 uM | kcat 1.23 s^-1 | kcat/Km 2.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 5.6 uM (standard error ± 0.2 uM); 1 uM is 0.001 mM, so 5.6 / 1000 = 0.0056 mM; the exported value is 0.0056 mM. kcat: printed Table 3 cell 1.23 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 1.23 s^(-1); the exported value is 1.23 s^(-1). kcat/Km: printed Table 3 cell 2.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^5 / 1000 = 220.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.23 / 0.0056 = 219.64285714285714 s^-1 mM^-1, the exported value, and 1.23 / 5.6 uM = 219600 M^-1 s^-1 rounds to the printed catalytic-efficiency cell 2.2 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 3, substrate row Cellotetraose: Km = 5.6 ± 0.2 uM; kcat = 1.23 s^-1; printed kcat/Km = 2.2 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row Cellotetraose


column_label: Table 3: Apparent kinetic constants for various electron donors with TtCDH (Biochimica et Biophysica Acta 2012, volume 1824, pages 802-812); printed column heads Substrate | Vmax (uM min^-1) | Km (uM) | kcat (s^-1) | kcat/Km (M^-1 s^-1). Table 3, substrate row Cellopentaose; column Vmax (uM min^-1) = 0.362 ± 0.003; column Km (uM) = 7.5 ± 0.2 uM; column kcat (s^-1) = 1.23; column kcat/Km (M^-1 s^-1) = 1.6 x 10^5. captured primary segment: Cellopentaose | Vmax 0.362 ± 0.003 uM min^-1 | Km 7.5 ± 0.2 uM | kcat 1.23 s^-1 | kcat/Km 1.6 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 7.5 uM (standard error ± 0.2 uM); 1 uM is 0.001 mM, so 7.5 / 1000 = 0.0075 mM; the exported value is 0.0075 mM. kcat: printed Table 3 cell 1.23 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 1.23 s^(-1); the exported value is 1.23 s^(-1). kcat/Km: printed Table 3 cell 1.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^5 / 1000 = 160.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.23 / 0.0075 = 164.0 s^-1 mM^-1, the exported value, and 1.23 / 7.5 uM = 164000 M^-1 s^-1 rounds to the printed catalytic-efficiency cell 1.6 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 3, substrate row Cellopentaose: Km = 7.5 ± 0.2 uM; kcat = 1.23 s^-1; printed kcat/Km = 1.6 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row Cellopentaose


column_label: Table 3: Apparent kinetic constants for various electron donors with TtCDH (Biochimica et Biophysica Acta 2012, volume 1824, pages 802-812); printed column heads Substrate | Vmax (uM min^-1) | Km (uM) | kcat (s^-1) | kcat/Km (M^-1 s^-1). Table 3, substrate row Cellotriose; column Vmax (uM min^-1) = 0.370 ± 0.005; column Km (uM) = 8.2 ± 0.4 uM; column kcat (s^-1) = 1.25; column kcat/Km (M^-1 s^-1) = 1.5 x 10^5. captured primary segment: Cellotriose | Vmax 0.370 ± 0.005 uM min^-1 | Km 8.2 ± 0.4 uM | kcat 1.25 s^-1 | kcat/Km 1.5 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 8.2 uM (standard error ± 0.4 uM); 1 uM is 0.001 mM, so 8.2 / 1000 = 0.0082 mM; the exported value is 0.0082 mM. kcat: printed Table 3 cell 1.25 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 1.25 s^(-1); the exported value is 1.25 s^(-1). kcat/Km: printed Table 3 cell 1.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^5 / 1000 = 150.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.25 / 0.0082 = 152.4390243902439 s^-1 mM^-1, the exported value, and 1.25 / 8.2 uM = 152400 M^-1 s^-1 rounds to the printed catalytic-efficiency cell 1.5 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 3, substrate row Cellotriose: Km = 8.2 ± 0.4 uM; kcat = 1.25 s^-1; printed kcat/Km = 1.5 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row Cellotriose


normalized_value_unit_evidence: Km=0.0039 mM; kcat=1.23 s^-1; printed kcat/Km=320 s^-1 mM^-1. The exported 315.3846153846154 is the derived 1.23/0.0039 quotient, not the explicit printed ratio.


column_label: Table label: Table 3 Apparent kinetic constants for various electron donors with TtCDH.. Row: Cellopentaose. Columns read: kcat (s^-1) cell 1.23, Km (uM) cell 7.5, kcat/Km (M^-1 s^-1) cell 1.6 x 10^5. metric: kcat; raw value: 1.23; raw unit: s^-1; normalized value: 1.23 s^(-1); metric: Km; raw value: 7.5; raw unit: uM; normalized value: 0.0075 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 164.0 s^-1 mM^-1, the quotient of this row's own kcat and Km cells; assay condition: Apparent kinetic constants for carbohydrate electron donors with purified recombinant TtCDH, determined with 110 uM DCPIP electron acceptor in 50 mM MES, pH 6.0; DCPIP is not saturating (Km = 78 uM); initial rate data fitted to the Michaelis-Menten equation with non-linear regression. Standard CDH activity assays monitored DCPIP absorbance at 600 nm at 25.0 C and were done in duplicate. Export row conditions: pH 6; 298.15 K.

normalized_value_unit_evidence: Table 3 row Cellopentaose: kcat 1.23 s^-1 = 1.23 s^(-1); Km 7.5 uM = 0.0075 mM (1 uM = 0.001 mM); kcat/Km 164.0 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells: 1.23 s^-1 / 7.5 uM = 164.0 s^-1 mM^-1. The paper's printed kcat/Km cell for this row, 1.6 x 10^5 M^-1 s^-1 = 160.0 s^-1 mM^-1, equals that quotient rounded at the printed cell's own two-significant-figure precision, so the two agree and the difference is printed precision only. In the PDF text layer superscript exponents are flattened, so the printed cell `1.6 × 105` is the paper's 1.6 x 10^5 M^-1 s^-1; the multiplication sign renders as ×, the superscript minus one as − 1, and the micro sign as μ.

raw_value_unit_evidence: Table 3 Apparent kinetic constants for various electron donors with TtCDH. | metric header rows of Table 3: `Substrate           Vmax                  Km                kcat         kcat/Km` with unit row `(μM min− 1)           (μM)              (s− 1)       (M− 1 s− 1)` (the U+2212 minus renders the paper's superscript -1, so the columns read Vmax (uM min^-1), Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1)) | row: Cellopentaose       0.362 ± 0.003         7.5 ± 0.2         1.23         1.6 × 105 | cells read: Vmax = 0.362 ± 0.003 uM min^-1; Km = 7.5 ± 0.2 uM; kcat = 1.23 s^-1; kcat/Km = 1.6 x 10^5 M^-1 s^-1

row_label: TtCDH | Cellopentaose


column_label: Table label: Table 3 Apparent kinetic constants for various electron donors with TtCDH.. Row: Cellotetraose. Columns read: kcat (s^-1) cell 1.23, Km (uM) cell 5.6, kcat/Km (M^-1 s^-1) cell 2.2 x 10^5. metric: kcat; raw value: 1.23; raw unit: s^-1; normalized value: 1.23 s^(-1); metric: Km; raw value: 5.6; raw unit: uM; normalized value: 0.0056 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 219.64285714285714 s^-1 mM^-1, the quotient of this row's own kcat and Km cells; assay condition: Apparent kinetic constants for carbohydrate electron donors with purified recombinant TtCDH, determined with 110 uM DCPIP electron acceptor in 50 mM MES, pH 6.0; DCPIP is not saturating (Km = 78 uM); initial rate data fitted to the Michaelis-Menten equation with non-linear regression. Standard CDH activity assays monitored DCPIP absorbance at 600 nm at 25.0 C and were done in duplicate. Export row conditions: pH 6; 298.15 K.

normalized_value_unit_evidence: Table 3 row Cellotetraose: kcat 1.23 s^-1 = 1.23 s^(-1); Km 5.6 uM = 0.0056 mM (1 uM = 0.001 mM); kcat/Km 219.64285714285714 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells: 1.23 s^-1 / 5.6 uM = 219.64285714285714 s^-1 mM^-1. The paper's printed kcat/Km cell for this row, 2.2 x 10^5 M^-1 s^-1 = 220.0 s^-1 mM^-1, equals that quotient rounded at the printed cell's own two-significant-figure precision, so the two agree and the difference is printed precision only. In the PDF text layer superscript exponents are flattened, so the printed cell `2.2 × 105` is the paper's 2.2 x 10^5 M^-1 s^-1; the multiplication sign renders as ×, the superscript minus one as − 1, and the micro sign as μ.

raw_value_unit_evidence: Table 3 Apparent kinetic constants for various electron donors with TtCDH. | metric header rows of Table 3: `Substrate           Vmax                  Km                kcat         kcat/Km` with unit row `(μM min− 1)           (μM)              (s− 1)       (M− 1 s− 1)` (the U+2212 minus renders the paper's superscript -1, so the columns read Vmax (uM min^-1), Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1)) | row: Cellotetraose       0.364 ± 0.003         5.6 ± 0.2         1.23         2.2 × 105 | cells read: Vmax = 0.364 ± 0.003 uM min^-1; Km = 5.6 ± 0.2 uM; kcat = 1.23 s^-1; kcat/Km = 2.2 x 10^5 M^-1 s^-1

row_label: TtCDH | Cellotetraose


column_label: Table label: Table 3 Apparent kinetic constants for various electron donors with TtCDH.. Row: Cellotriose. Columns read: kcat (s^-1) cell 1.25, Km (uM) cell 8.2, kcat/Km (M^-1 s^-1) cell 1.5 x 10^5. metric: kcat; raw value: 1.25; raw unit: s^-1; normalized value: 1.25 s^(-1); metric: Km; raw value: 8.2; raw unit: uM; normalized value: 0.0082 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 152.4390243902439 s^-1 mM^-1, the quotient of this row's own kcat and Km cells; assay condition: Apparent kinetic constants for carbohydrate electron donors with purified recombinant TtCDH, determined with 110 uM DCPIP electron acceptor in 50 mM MES, pH 6.0; DCPIP is not saturating (Km = 78 uM); initial rate data fitted to the Michaelis-Menten equation with non-linear regression. Standard CDH activity assays monitored DCPIP absorbance at 600 nm at 25.0 C and were done in duplicate. Export row conditions: pH 6; 298.15 K.

normalized_value_unit_evidence: Table 3 row Cellotriose: kcat 1.25 s^-1 = 1.25 s^(-1); Km 8.2 uM = 0.0082 mM (1 uM = 0.001 mM); kcat/Km 152.4390243902439 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells: 1.25 s^-1 / 8.2 uM = 152.4390243902439 s^-1 mM^-1. The paper's printed kcat/Km cell for this row, 1.5 x 10^5 M^-1 s^-1 = 150.0 s^-1 mM^-1, equals that quotient rounded at the printed cell's own two-significant-figure precision, so the two agree and the difference is printed precision only. In the PDF text layer superscript exponents are flattened, so the printed cell `1.5 × 105` is the paper's 1.5 x 10^5 M^-1 s^-1; the multiplication sign renders as ×, the superscript minus one as − 1, and the micro sign as μ.

raw_value_unit_evidence: Table 3 Apparent kinetic constants for various electron donors with TtCDH. | metric header rows of Table 3: `Substrate           Vmax                  Km                kcat         kcat/Km` with unit row `(μM min− 1)           (μM)              (s− 1)       (M− 1 s− 1)` (the U+2212 minus renders the paper's superscript -1, so the columns read Vmax (uM min^-1), Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1)) | row: Cellotriose         0.370 ± 0.005         8.2 ± 0.4         1.25         1.5 × 105 | cells read: Vmax = 0.370 ± 0.005 uM min^-1; Km = 8.2 ± 0.4 uM; kcat = 1.25 s^-1; kcat/Km = 1.5 x 10^5 M^-1 s^-1

row_label: TtCDH | Cellotriose


column_label: Table II; row Cellotetraose; columns Km, kcat, and kcat/Km; exact cells 61 x 10^-3 mM, 20.7 s^-1, and 339 mM^-1 s^-1.

raw_value_unit_evidence: Table II cellotetraose row: Km 61 x 10^-3 mM; kcat 20.7 s^-1; kcat/Km 339 mM^-1 s^-1.

row_label: cellotetraose

table_label: Table II: Specificity of CDH for Substrates and Electron Acceptors


column_label: Table II; row Cellopentaose; columns Km, kcat, and kcat/Km; exact cells 55 x 10^-3 mM, 21.5 s^-1, and 391 mM^-1 s^-1.

raw_value_unit_evidence: Table II cellopentaose row: Km 55 x 10^-3 mM; kcat 21.5 s^-1; kcat/Km 391 mM^-1 s^-1.

row_label: cellopentaose


column_label: Table II; row Cellotriose; columns Km, kcat, and kcat/Km; exact cells 62 x 10^-3 mM, 24 s^-1, and 387 mM^-1 s^-1.

raw_value_unit_evidence: Table II cellotriose row: Km 62 x 10^-3 mM; kcat 24 s^-1; kcat/Km 387 mM^-1 s^-1.

row_label: cellotriose


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M685Y with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


proof_lines:
Phanerochaete chrysosporium
PcCDH
cellobiose dehydrogenase


organism: Ensifer sp. AS08

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H465A to reconstruct the assayed variant sequence.

smiles: OCCO


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N90A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: triiodide ion

smiles: I[I-]I

substrate: triiodide ion


organism: Homo sapiens

substrate_name: GHB

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

column_label: Results prose reports apparent Km values of 0.17 mmol/L and 1.2 mmol/L for GHB and 2-KG respectively; Table 1 lists GHB human liver 0.2 x 10^-3 mol/L, consistent with the rounded prose value.

raw_value_unit_evidence: Km raw_value=0.17 raw_unit=mmol/L

row_label: GHB / Human liver

table_label: Results prose and Table 1: apparent Km values

substrate: GHB


substrate_name: SSA

column_label: Results prose reports apparent Km values of 0.04 mmol/L and 0.12 mmol/L for SSA and D-2-HG respectively; Table 1 lists SSA human liver 0.4 x 10^-4 mol/L, equal to 0.04 mM.

raw_value_unit_evidence: Km raw_value=0.04 raw_unit=mmol/L

row_label: SSA / Human liver

substrate: SSA


enzyme_display_name: UniProt Q3L245

organism: Leucoagaricus meleagris

substrate_name: L-arabinose

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q3L245

substrate: L-arabinose


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=8.5


substrate_name: D-mannose

substrate: D-mannose


substrate_name: maltotriose

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

substrate: maltotriose


substrate_name: L-sorbose

substrate: L-sorbose


substrate_name: methyl-alpha-D-glucopyranoside

substrate: methyl-alpha-D-glucopyranoside


substrate_name: D-sorbose

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

substrate: D-sorbose


substrate_name: xylobiose

substrate: xylobiose


enzyme_display_name: Pyranose dehydrogenase

organism: Agaricus bisporus

substrate_name: D-glucose (with 1,4-benzoquinone as electron acceptor)

enzyme: Pyranose dehydrogenase


substrate_name: D-cellobiose (with 1,4-benzoquinone as electron acceptor)


substrate_name: L-arabinose (with 1,4-benzoquinone as electron acceptor)


substrate_name: sucrose (with 1,4-benzoquinone as electron acceptor)


substrate_name: 1,4-benzoquinone (with D-glucose as substrate)


enzyme_display_name: (S)-mandelate dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: (S)-Mandelate

enzyme: (S)-mandelate dehydrogenase

substrate: (S)-Mandelate


substrate_name: ferricyanide


organism: Chaetomium sp.

substrate_name: cellobiose

substrate: cellobiose


organism: Irpex lacteus


organism: Rattus norvegicus

substrate_name: GHB

column_label: Printed page 16878, Table X, gamma-hydroxybutyrate row, Km(app) column: 3.0 x 10^-4 M.

normalized_value_unit_evidence: 3.0 x 10^-4 M = 0.3 mM; exact match to the current row.

raw_value_unit_evidence: Km(app) = 3.0 x 10^-4 M for gamma-hydroxybutyrate.

row_label: gamma-hydroxybutyrate

table_label: Table X


substrate_name: SSA


organism: Termitomyces sp. OE 147

substrate_name: maltose

proof_lines:
cellobiose
pH 5.0
cellulose degradation


proof_lines:
cellobiose
ferricytochrome c
DCIP


substrate_name: lactose

proof_lines:
lactose
DCIP
cytochrome c


substrate_name: benzyl viologen

proof_lines:
cellobiose oxidase
substrate specificity
Phanerodontia chrysosporium

substrate: benzyl viologen


enzyme_display_name: 2-oxo-acid reductase

organism: Proteus mirabilis

substrate_name: carboxamido-methyl viologen

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

enzyme: 2-oxo-acid reductase

substrate: carboxamido-methyl viologen


substrate_name: D-ribonate

substrate: D-ribonate


substrate_name: galactarate

substrate: galactarate


substrate_name: D-galactonate

substrate: D-galactonate


substrate_name: D-gulonate

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

substrate: D-gulonate


substrate_name: Lactobionate

substrate: Lactobionate


substrate_name: D-lactate

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

substrate: D-lactate


substrate_name: L-arabinuronate

substrate: L-arabinuronate


substrate_name: D-glucarate

substrate: D-glucarate


enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Macropsalliota meleagris

substrate_name: D-galactose

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

enzyme: pyranose dehydrogenase (acceptor)

substrate: D-galactose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: cellobiose


substrate_name: ferrocenium ion

proof_lines: mutant enzyme N75G/N175Q, at pH 7.5 and 30°C

substrate: ferrocenium ion


proof_lines: mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C


proof_lines: mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C


proof_lines: mutant enzyme N75G/N252Q, at pH 7.5 and 30°C


proof_lines: wild type enzyme, with D-glucose as cosubstrate, at pH 8.5 and 30°C


substrate_name: D-sorbose

substrate: D-sorbose


substrate_name: D-trehalose

substrate: D-trehalose


substrate_name: sucrose

substrate: sucrose


substrate_name: D-maltoheptaose

substrate: D-maltoheptaose


substrate_name: D-maltopentaose

substrate: D-maltopentaose


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


substrate_name: D-glucosamine

substrate: D-glucosamine


substrate_name: L-fucose

substrate: L-fucose


assay_conditions_summary: pH 4; 303.15 K; cofactor FAD

proof_lines: mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C


substrate_name: lactose

assay_conditions_summary: pH 8.5; 303.15 K; cofactor FAD

proof_lines: mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C

substrate: lactose


proof_lines: mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 8.5 and 30°C


substrate_name: D-glucose

substrate: D-glucose


proof_lines: wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C


smiles: O=O

proof_lines: wild type enzyme, with D-glucose as cosubstrate, at pH 7.4 and 30°C


assay_conditions_summary: pH 7.4; 303.15 K; cofactor FAD

proof_lines: mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 7.4 and 30°C


substrate_name: L-sorbose

proof_lines: with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication

substrate: L-sorbose


substrate_name: xylobiose

substrate: xylobiose


substrate_name: maltose

assay_conditions_summary: pH 7.5; 303.15 K; buffer phosphate

proof_lines: isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

proof_lines: isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

proof_lines: recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5

substrate: maltose


substrate_name: methyl-alpha-D-glucopyranoside

proof_lines: isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

substrate: methyl-alpha-D-glucopyranoside


assay_conditions_summary: pH 4; 303.15 K; buffer phosphate

proof_lines: isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C

proof_lines: isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C

proof_lines: recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0


proof_lines: isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C


substrate_name: maltotriose

substrate: maltotriose


substrate_name: D-xylose

substrate: D-xylose


enzyme_display_name: (R)-pantolactone dehydrogenase (flavin)

organism: Nocardia asteroides

substrate_name: (R)-pantolactone

enzyme: (R)-pantolactone dehydrogenase (flavin)

substrate: (R)-pantolactone


substrate_name: D-xylobiose

substrate: D-xylobiose


proof_lines: mutant enzyme N75G/N175Q, at pH 7.5 and 30°C


substrate_name: D-mannose

substrate: D-mannose


proof_lines: mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C


proof_lines: wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C


substrate_name: cellobiose

substrate: cellobiose


proof_lines: mutant enzyme N75G/N252Q, at pH 7.5 and 30°C


proof_lines: mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C


organism: Escherichia coli

substrate_name: (S)-Mandelate

proof_lines: chitosan-immobilized enzyme, at pH 3.4 and 45°C

substrate: (S)-Mandelate


substrate_name: D-allose

substrate: D-allose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: ferricenium ion

substrate: ferricenium ion


substrate_name: D-Mannose

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

substrate: D-Mannose


substrate_name: D-Xylose

substrate: D-Xylose


organism: Chlorophyllum rhacodes

substrate_name: D-glucose

proof_lines: 25°C, ferricenium ion as electron acceptor

substrate: D-glucose


substrate_name: L-arabinose

substrate: L-arabinose


organism: Agaricus xanthodermus

source_databases_merged: brenda uniprot


substrate_name: ferricenium hexafluorophosphate

substrate: ferricenium hexafluorophosphate


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: D-arabinose

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

proof_lines: at 30°C with 0.4 mM ferricenium as electron acceptor

substrate: D-arabinose


substrate_name: gentiobiose

substrate: gentiobiose


substrate_name: D-maltotriose

substrate: D-maltotriose


organism: Pseudomonas putida

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

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

proof_lines: pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach


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


smiles: CCCCC(C(=O)[O-])O


smiles: CCCC(C(=O)[O-])O


smiles: CCCCCCC(C(=O)[O-])O


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


smiles: CCOC(=O)C(C#C)O


substrate_name: 2-hydroxybutanoate (at pH 7.5 and 20 degrees Celsius)

proof_lines: kcat is 290 sec(-1) with (S)-mandelate as substrate and DCPIP as electron acceptor (at pH 7.5 and 20 degrees Celsius) (PubMed:10493804). kcat is 0.5 sec(-1) with 2-hydroxyoctanoate as substrate and DCPIP as electron acceptor (at pH 7.5 and


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165G/R277K to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R277G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5


sequence_variant_note: Mutation signature R165K/R277K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


proof_lines: mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R277L to reconstruct the assayed variant sequence.


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


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

column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `DCIP (pH 4)` the AxPDH group prints Km 0.09, kcat 7.65 and kcat/Km 85.0.

normalized_value_unit_evidence: kcat: printed Table 4 cell 7.65 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 7.65 s^(-1). Km: printed cell 0.09 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.09 mM. kcat/Km: printed cell 85.0 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 85.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 7.65 / 0.09 = 85.0 s^-1 mM^-1, against the printed efficiency cell 85.0.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `DCIP (pH 4)`, AxPDH column group: Km = 0.09 mM; kcat = 7.65 s-1; kcat/Km = 85.0 mM-1 s-1.

row_label: Table 4, substrate row `DCIP (pH 4)`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)

table_label: Table 4: Apparent kinetic constants for selected electron acceptors determined at 30 °C with 25 mM D-glucose as the electron donor. (Biomolecules 2013, 3(3):535-552)


column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `1,4-BQ (pH 4)` the AxPDH group prints Km 3.25, kcat 12.89 and kcat/Km 4.0.

normalized_value_unit_evidence: kcat: printed Table 4 cell 12.89 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 12.89 s^(-1). Km: printed cell 3.25 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 3.25 mM. kcat/Km: printed cell 4.0 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 4.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 12.89 / 3.25 = 3.9661538461538464 s^-1 mM^-1, against the printed efficiency cell 4.0.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `1,4-BQ (pH 4)`, AxPDH column group: Km = 3.25 mM; kcat = 12.89 s-1; kcat/Km = 4.0 mM-1 s-1.

row_label: Table 4, substrate row `1,4-BQ (pH 4)`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)


assay_conditions_summary: pH 7.5; 303.15 K; buffer the standard activity assay: 50 mM sodium phosphate

column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `D-glucose` the AxPDH group prints Km 0.49, kcat 13.02 and kcat/Km 26.6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13.02 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 13.02 s^(-1). Km: printed cell 0.49 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.49 mM. kcat/Km: printed cell 26.6 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 26.6 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 13.02 / 0.49 = 26.57142857142857 s^-1 mM^-1, against the printed efficiency cell 26.6.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `D-glucose`, AxPDH column group: Km = 0.49 mM; kcat = 13.02 s-1; kcat/Km = 26.6 mM-1 s-1.

row_label: Table 3, substrate row `D-glucose`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)

table_label: Table 3: Apparent kinetic constants for selected electron donors determined at 30 °C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor. (Biomolecules 2013, 3(3):535-552)


column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `L-arabinose` the AxPDH group prints Km 4.16, kcat 22.90 and kcat/Km 5.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22.90 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 22.9 s^(-1). Km: printed cell 4.16 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 4.16 mM. kcat/Km: printed cell 5.5 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 5.5 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 22.9 / 4.16 = 5.504807692307692 s^-1 mM^-1, against the printed efficiency cell 5.5.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `L-arabinose`, AxPDH column group: Km = 4.16 mM; kcat = 22.90 s-1; kcat/Km = 5.5 mM-1 s-1.

row_label: Table 3, substrate row `L-arabinose`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)


substrate_name: lactose

proof_lines: with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

substrate: lactose


assay_conditions_summary: pH 5; buffer phosphate

proof_lines: recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0

proof_lines: native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0


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

assay_conditions_summary: pH 7.5; 293.15 K; buffer 0.1 M potassium phosphate

proof_lines: in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C

source_databases_merged: brenda skid uniprot


proof_lines: pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach

proof_lines: pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with 205 residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach


sequence_source: multiple

proof_lines: pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted

proof_lines: pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus


proof_lines: pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, wild-type enzyme


organism: Rhodotorula graminis

proof_lines: pH 7.5, 25°C, electron acceptor: 2,6-dichloroindophenol

proof_lines: pH 7.5, 25°C, electron acceptor: cytochrome c

proof_lines: pH 7.5, 25°C, electron acceptor: ferricyanide


organism: Agaricus campestris

column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `L-arabinose` the AcPDH group prints Km 4.23, kcat 3.05 and kcat/Km 0.7.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.05 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 3.05 s^(-1). Km: printed cell 4.23 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 4.23 mM. kcat/Km: printed cell 0.7 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 0.7 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 3.05 / 4.23 = 0.7210401891252954 s^-1 mM^-1, against the printed efficiency cell 0.7.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `L-arabinose`, AcPDH column group: Km = 4.23 mM; kcat = 3.05 s-1; kcat/Km = 0.7 mM-1 s-1.

row_label: Table 3, substrate row `L-arabinose`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)


column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `Lactose` the AcPDH group prints Km 53.16, kcat 3.12 and kcat/Km 0.1.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.12 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 3.12 s^(-1). Km: printed cell 53.16 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 53.16 mM. kcat/Km: printed cell 0.1 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 0.1 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 3.12 / 53.16 = 0.058690744920993236 s^-1 mM^-1, against the printed efficiency cell 0.1.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `Lactose`, AcPDH column group: Km = 53.16 mM; kcat = 3.12 s-1; kcat/Km = 0.1 mM-1 s-1.

row_label: Table 3, substrate row `Lactose`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 °C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor. Enzyme column group 'AcPDH'; substrate row 'D-glucose'; column 'Km [mM]' = 0.35; column 'kcat [s-1]' = 4.10; column 'kcat/Km [mM-1 s-1]' = 11.7.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.35, header unit mM; already millimolar, no conversion; the exported value is 0.35 mM. kcat: printed Table 3 cell 4.10, header unit s^-1; no conversion; the exported value is 5.23 s^(-1). kcat/Km: printed Table 3 cell 11.7, header unit mM^-1 s^-1, which is the export's own ratio unit; no conversion; the exported value is 14.942857142857145 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme column group 'AcPDH', substrate row 'D-glucose': Km = 0.35 mM; kcat = 4.10 s^-1; printed kcat/Km = 11.7 mM^-1 s^-1.


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 °C with 25 mM D-glucose as the electron donor. Enzyme column group 'AcPDH'; substrate row 'DCIP (pH 4)'; column 'Km [mM]' = 0.11; column 'kcat [s-1]' = 10.56; column 'kcat/Km [mM-1 s-1]' = 96.0.

normalized_value_unit_evidence: Km: printed Table 4 cell 0.11, header unit mM; already millimolar, no conversion; the exported value is 0.00011 mM. kcat: printed Table 4 cell 10.56, header unit s^-1; no conversion; the exported value is 10.56 s^(-1). kcat/Km: printed Table 4 cell 96.0, header unit mM^-1 s^-1, which is the export's own ratio unit; no conversion; the exported value is 96000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, enzyme column group 'AcPDH', substrate row 'DCIP (pH 4)': Km = 0.11 mM; kcat = 10.56 s^-1; printed kcat/Km = 96.0 mM^-1 s^-1.


column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `1,4-BQ (pH 4)` the AcPDH group prints Km 0.12, kcat 34.82 and kcat/Km 302.8.

normalized_value_unit_evidence: kcat: printed Table 4 cell 34.82 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 34.82 s^(-1). Km: printed cell 0.12 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.12 mM. kcat/Km: printed cell 302.8 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 302.8 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 34.82 / 0.12 = 290.1666666666667 s^-1 mM^-1, against the printed efficiency cell 302.8.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `1,4-BQ (pH 4)`, AcPDH column group: Km = 0.12 mM; kcat = 34.82 s-1; kcat/Km = 302.8 mM-1 s-1.

row_label: Table 4, substrate row `1,4-BQ (pH 4)`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H274G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H274G, in presence of 20 mM imidazole


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81D to reconstruct the assayed variant sequence.

source_databases_merged: brenda oed


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81V to reconstruct the assayed variant sequence.


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxybutyrate. Cells read: kcat cell 0.10 ± 0.01 s-1 and Km cell 32.0 ± 3.5 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.10 ± 0.01 s-1 equals the exported kcat 0.1 s^(-1) with no unit conversion; Km 32.0 ± 3.5 mM equals the exported km 32.0 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.003 s-1 mM-1; the exported ratio 0.003125 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxybutyrate: kcat 0.10 ± 0.01 s-1 = 0.1 s^(-1) (no conversion); Km 32.0 ± 3.5 mM = 32.0 mM (no conversion); kcat/Km 0.003125 s^-1 mM^-1 = 0.1 / 32.0.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxybutyrate	0.10 ± 0.01	32.0 ± 3.5	0.003	0.37 ± 0.03	4.4 ± 1.0	0.08 | the line's leading label is wtMDH | 2-hydroxybutyrate

row_label: wtMDH | 2-hydroxybutyrate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH


proof_lines:
pH 7.5, 20°C, mutant enzyme G81A
mutant G81A
mutant G81A of chimera MDH-GOX2


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyhexanoate. Cells read: kcat cell 0.34 ± 0.02 s-1 and Km cell 4.9 ± 0.4 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.34 ± 0.02 s-1 equals the exported kcat 0.34 s^(-1) with no unit conversion; Km 4.9 ± 0.4 mM equals the exported km 4.9 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.07 s-1 mM-1; the exported ratio 0.06938775510204082 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxyhexanoate: kcat 0.34 ± 0.02 s-1 = 0.34 s^(-1) (no conversion); Km 4.9 ± 0.4 mM = 4.9 mM (no conversion); kcat/Km 0.06938775510204082 s^-1 mM^-1 = 0.34 / 4.9.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyhexanoate	0.34 ± 0.02	4.9 ± 0.4	0.07	0.19 ± 0.008	1.4 ± 0.2	0.14 | the line's leading label is wtMDH | 2-hydroxyhexanoate

row_label: wtMDH | 2-hydroxyhexanoate


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyvalerate. Cells read: kcat cell 0.36 ± 0.01 s-1 and Km cell 15.3 ± 1.5 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.36 ± 0.01 s-1 equals the exported kcat 0.36 s^(-1) with no unit conversion; Km 15.3 ± 1.5 mM equals the exported km 15.3 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.024 s-1 mM-1; the exported ratio 0.023529411764705882 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyvalerate	0.36 ± 0.01	15.3 ± 1.5	0.024	0.27 ± 0.02	6.4 ± 1.0	0.04 | the line's leading label is wtMDH | 2-hydroxyvalerate

row_label: wtMDH | 2-hydroxyvalerate


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyoctanoate. Cells read: kcat cell 0.5 ± 0.06 s-1 and Km cell 0.8 ± 0.1 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.5 ± 0.06 s-1 equals the exported kcat 0.5 s^(-1) with no unit conversion; Km 0.8 ± 0.1 mM equals the exported km 0.8 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.63 s-1 mM-1; the exported ratio 0.625 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxyoctanoate: kcat 0.5 ± 0.06 s-1 = 0.5 s^(-1) (no conversion); Km 0.8 ± 0.1 mM = 0.8 mM (no conversion); kcat/Km 0.625 s^-1 mM^-1 = 0.5 / 0.8.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyoctanoate	0.5 ± 0.06	0.8 ± 0.1	0.63	0.26 ± 0.01	0.14 ± 0.01	1.9 | the line's leading label is wtMDH | 2-hydroxyoctanoate

row_label: wtMDH | 2-hydroxyoctanoate


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81S to reconstruct the assayed variant sequence.


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyisocaproate. Cells read: kcat cell 0.8 ± 0.05 s-1 and Km cell 4.3 ± 0.2 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.8 ± 0.05 s-1 equals the exported kcat 0.8 s^(-1) with no unit conversion; Km 4.3 ± 0.2 mM equals the exported km 4.3 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.19 s-1 mM-1; the exported ratio 0.186046511627907 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxyisocaproate: kcat 0.8 ± 0.05 s-1 = 0.8 s^(-1) (no conversion); Km 4.3 ± 0.2 mM = 4.3 mM (no conversion); kcat/Km 0.186046511627907 s^-1 mM^-1 = 0.8 / 4.3.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyisocaproate	0.8 ± 0.05	4.3 ± 0.2	0.19	0.48 ± 0.02	1.6 ± 0.1	0.3 | the line's leading label is wtMDH | 2-hydroxyisocaproate

row_label: wtMDH | 2-hydroxyisocaproate


column_label: Table: Table 3:  wtMDH and the Gly81 Mutants:  Activities with Oxygen as the Electron Acceptor and Redox Potentialsa Printed line read: wtMDH. Cells read: kcat cell 1.2 ± 0.7 s-1 and Km cell 3.2 ± 1.9 mM. Both cells were read from the single printed wtMDH line of this table; the remaining printed cells on that line (kox, Kd(O2), redox potential) were not used. kcat 1.2 ± 0.7 s-1 equals the exported kcat 1.2 s^(-1) with no unit conversion; Km 3.2 ± 1.9 mM equals the exported km 3.2 mM with no unit conversion. This table prints no kcat/Km cell, so the exported ratio is recorded only as the quotient of this line's own two printed cells. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

raw_value_unit_evidence: Table 3:  wtMDH and the Gly81 Mutants:  Activities with Oxygen as the Electron Acceptor and Redox Potentialsa | printed line: wtMDH	1.2 ± 0.7	3.2 ± 1.9	2.5 ± 0.9	2.3 ± 0.9	−91 ± 4 | the line's leading label is wtMDH

row_label: wtMDH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81S to reconstruct the assayed variant sequence.


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxy-3-butynoate. Cells read: kcat cell 3.9 ± 0.1 s-1 and Km cell 22.0 ± 1.5 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 3.9 ± 0.1 s-1 equals the exported kcat 3.9 s^(-1) with no unit conversion; Km 22.0 ± 1.5 mM equals the exported km 22.0 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.177 s-1 mM-1; the exported ratio 0.17727272727272728 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxy-3-butynoate: kcat 3.9 ± 0.1 s-1 = 3.9 s^(-1) (no conversion); Km 22.0 ± 1.5 mM = 22.0 mM (no conversion); kcat/Km 0.17727272727272728 s^-1 mM^-1 = 3.9 / 22.0.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxy-3-butynoate	3.9 ± 0.1	22.0 ± 1.5	0.177	14.8 ±0.6	4.3 ± 0.5	3.4 | the line's leading label is wtMDH | 2-hydroxy-3-butynoate

row_label: wtMDH | 2-hydroxy-3-butynoate


substrate_name: Phenyllactate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81A to reconstruct the assayed variant sequence.

substrate: Phenyllactate


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 3-phenyllactate. Cells read: kcat cell 0.52 ± 0.01 s-1 and Km cell 2.0 ± 0.1 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.52 ± 0.01 s-1 equals the exported kcat 0.52 s^(-1) with no unit conversion; Km 2.0 ± 0.1 mM equals the exported km 2.0 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.26 s-1 mM-1; the exported ratio 0.26 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 3-phenyllactate: kcat 0.52 ± 0.01 s-1 = 0.52 s^(-1) (no conversion); Km 2.0 ± 0.1 mM = 2.0 mM (no conversion); kcat/Km 0.26 s^-1 mM^-1 = 0.52 / 2.0.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 3-phenyllactate	0.52 ± 0.01	2.0 ± 0.1	0.26	0.15 ± 0.002	0.37 ± 0.02	0.4 | the line's leading label is wtMDH | 3-phenyllactate

row_label: wtMDH | 3-phenyllactate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81V to reconstruct the assayed variant sequence.


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


raw_value_unit_evidence: Table 2 reports 2-hydroxyvalerate row, wtMDH columns: kcat (0.36 +/- 0.01) s^-1, Km (15.3 +/- 1.5) mM, kcat/Km 0.024 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: 2-hydroxyvalerate row / wtMDH columns

table_label: Table 2 / Comparison of Substrate Specificity of wtMDH and G81A


raw_value_unit_evidence: Table 2 reports 4-chloromandelate row, wtMDH columns: kcat (334 +/- 6) s^-1, Km (0.27 +/- 0.04) mM, kcat/Km 1237 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: 4-chloromandelate row / wtMDH columns


substrate_name: Indoleglycolate

substrate: Indoleglycolate


raw_value_unit_evidence: Table 2 reports indoleglycolate row, wtMDH columns: kcat (122 +/- 14) s^-1, Km (0.40 +/- 0.03) mM, kcat/Km 305 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: indoleglycolate row / wtMDH columns


substrate_name: Indolelactate

substrate: Indolelactate


raw_value_unit_evidence: Table 2 reports 3-indolelactate row, wtMDH columns: kcat (1.0 +/- 0.01) s^-1, Km (0.9 +/- 0.1) mM, kcat/Km 1.1 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: 3-indolelactate row / wtMDH columns


substrate_name: Mandelate

substrate: Mandelate


raw_value_unit_evidence: Table 2 reports mandelate row, wtMDH columns: kcat (350 +/- 10) s^-1, Km (0.24 +/- 0.02) mM, kcat/Km 1458 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: mandelate row / wtMDH columns


substrate_name: (S)-Mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R165E to reconstruct the assayed variant sequence.

substrate: (S)-Mandelate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature R165G/R277K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


sequence_variant_note: Mutation signature R165K/R277G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature R165K/R277K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R277G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R277K to reconstruct the assayed variant sequence.


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


column_label: ScienceDirect article HTML, Table 2; row 2,6-Dichloroindophenol (2 e-) (pH 4); Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=0.06 mM; kcat=57.6 s^-1; printed kcat/Km=958 s^-1 mM^-1; exported kcat/Km=960.0000000000001 s^-1 mM^-1.

row_label: 2,6-Dichloroindophenol (2 e-) (pH 4)

table_label: Table 2


substrate_name: cellobiose

column_label: ScienceDirect article HTML, Table 2; row Cellobiose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=2.45 mM; kcat=24.63 s^-1; printed kcat/Km=10 s^-1 mM^-1; exported kcat/Km=10.461224489795917 s^-1 mM^-1. Exported kcat=25.63 s^-1 but Table 2 prints 24.63 s^-1.

row_label: Cellobiose

substrate: cellobiose


substrate_name: D-galactose

column_label: ScienceDirect article HTML, Table 2; row d-Galactose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=4.19 mM; kcat=28.7 s^-1; printed kcat/Km=6.9 s^-1 mM^-1; exported kcat/Km=6.849642004773269 s^-1 mM^-1.

row_label: d-Galactose

substrate: D-galactose


column_label: ScienceDirect article HTML, Table 2; row d-Glucose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=1.54 mM; kcat=33.7 s^-1; printed kcat/Km=22 s^-1 mM^-1; exported kcat/Km=21.883116883116884 s^-1 mM^-1.

row_label: d-Glucose


substrate_name: ferrocenium ion

substrate: ferrocenium ion


substrate_name: D-Xylose

column_label: ScienceDirect article HTML, Table 2; row d-Xylose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=4.75 mM; kcat=36.9 s^-1; printed kcat/Km=7.8 s^-1 mM^-1; exported kcat/Km=7.768421052631578 s^-1 mM^-1.

row_label: d-Xylose

substrate: D-Xylose


column_label: ScienceDirect article HTML, Table 2; row Lactose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=40.51 mM; kcat=15.95 s^-1; printed kcat/Km=0.4 s^-1 mM^-1; exported kcat/Km=0.3937299432238953 s^-1 mM^-1.

row_label: Lactose


substrate_name: maltose

column_label: ScienceDirect article HTML, Table 2; row Maltose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=2.16 mM; kcat=27.26 s^-1; printed kcat/Km=13 s^-1 mM^-1; exported kcat/Km=12.62037037037037 s^-1 mM^-1.

row_label: Maltose

substrate: maltose


substrate_name: raffinose

column_label: ScienceDirect article HTML, Table 2; row Raffinose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=10.79 mM; kcat=19.61 s^-1; printed kcat/Km=1.8 s^-1 mM^-1; exported kcat/Km=1.8174235403151067 s^-1 mM^-1.

row_label: Raffinose

substrate: raffinose


substrate_name: D-Mannose

column_label: ScienceDirect article HTML, Table 2; row d-Mannose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=109.1 mM; kcat=13.31 s^-1; printed kcat/Km=0.1 s^-1 mM^-1; exported kcat/Km=0.12199816681943172 s^-1 mM^-1.

row_label: d-Mannose

substrate: D-Mannose


column_label: ScienceDirect article HTML, Table 2; row 1,4-Benzoquinone (2 e-) (pH 4); Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=0.566 mM; kcat=44.2 s^-1; printed kcat/Km=78 s^-1 mM^-1; exported kcat/Km=78.09187279151945 s^-1 mM^-1.

row_label: 1,4-Benzoquinone (2 e-) (pH 4)