organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 7.8; 321.15 K; cofactor NADPH

column_label: Table 1 (Activities of wild type and mutants of ST0318), FBPase block, row 'Wild type'; column 'kcat (s^-1)' = 0.62; column 'Km (mM)' = 0.027; column 'kcat/Km (s^-1 mM^-1)' = 23. The kcat and Km cells also print the standard deviations 0.02 and 0.003, which the export does not carry.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.62 s^-1; already in s^-1, so no unit conversion applies; the value carried forward is 0.62 s^(-1). Km: printed Table 1 cell 0.027 mM; already in mM, so no unit conversion applies; the value carried forward is 0.027 mM. kcat/Km: the printed Table 1 cell 23 s^-1 mM^-1 is the rounded rendering of the exact same-row quotient 0.62 / 0.027 = 22.962962962962962 s^(-1)*mM^(-1), and that exact quotient is the value carried forward.

raw_value_unit_evidence: Table 1, FBPase block, row 'Wild type': kcat = 0.62 s^-1; Km = 0.027 mM; printed kcat/Km = 23 s^-1 mM^-1.

row_label: Table 1, FBPase block, row 'Wild type'


enzyme_display_name: fructose-bisphosphatase

substrate_name: D-fructose 1,6-bisphosphate

source_db: oed

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

enzyme: fructose-bisphosphatase

substrate: D-fructose 1,6-bisphosphate

source: oed


source_db: skid

verification_status: verified

mutation_signature: Unknown

source_license: CC BY-NC-ND 4.0

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

status: verified

source: skid


organism: Sus scrofa

substrate_name: Fructose 1,6-bisphosphate; H2O

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

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Tyr57Trp

substrate: Fructose 1,6-bisphosphate; H2O


substrate_name: H2O; D-Fructose 1,6-bisphosphate

km_display: Not reported

ki_unit: mM

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Glu-tagged

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Glu97->Ala(1 3)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp118->Ala(1 3)

substrate: H2O; D-Fructose 1,6-bisphosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant T27A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E192A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E192Q


substrate_name: D-Fructose 1,6-bisphosphate

substrate: D-Fructose 1,6-bisphosphate


substrate_name: D-Fructose 1,6-bisphosphate; H2O

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant D187A

substrate: D-Fructose 1,6-bisphosphate; H2O


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Lys71Ala


organism: Synechocystis sp.


verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

status: unverified


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


organism: Thermotoga maritima

substrate_name: H2O; Fructose 1,6-bisphosphate

substrate: H2O; Fructose 1,6-bisphosphate


organism: Vigna radiata

kcat_display: Not reported

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R30T/D32E/F33L


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R30T/D32E


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant M251L


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant D32E


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant D32E/D33L


organism: Homo sapiens

source_db: brenda

proof_lines:
wild-type liver isoenzyme enzyme
wild-type liver enzyme, pH 7.5, 37°C
wild-type, pH 7.0, 37°C

source: brenda


substrate_name: fructose 1,6-diphosphate

proof_lines:
alkaline isoenzyme
neutral isoenzyme
pH 7.5, 30°C, recombinant enzyme

substrate: fructose 1,6-diphosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp74Glu


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asn64Ala


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp74Ala


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asn64Gln


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp68Glu


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp74Asn


organism: Synechococcus elongatus

substrate_name: H2O; beta-D-Fructose 1,6-bisphosphate

substrate: H2O; beta-D-Fructose 1,6-bisphosphate


organism: Euglena gracilis

assay_conditions_summary: pH 8

proof_lines: isozyme EgFBPaseI, pH 8.0, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication

proof_lines: isozyme EgFBPaseII, pH 8.0, temperature not specified in the publication


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R15A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R22K


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E19Q


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R22M


organism: Synechococcus sp.

proof_lines:
isoenzyme F-II
isoenzyme F-I


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

substrate_name: inositol-1-phosphate (at 85 degrees Celsius)

source_db: uniprot

proof_lines: kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius) and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius).

source: uniprot


organism: Cenarchaeum symbiosum (strain A)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius)

proof_lines: The aldolase reaction is a classic case for a fully reversible enzymatic reaction but here, the KM values for the substrate for the aldol condensation and the aldol cleavage differ by a factor of 1000, and the intrinsic phosphatase activity


organism: Escherichia coli (strain K12)

substrate_name: fructose 1,6-bisphosphate (at pH 7.7 and room temperature)

proof_lines: The catalytic efficiency of GlpX is 3-fold higher than that of YggF, the other FBPase class 2 in E.coli.


substrate_name: fructose 1,6-bisphosphate

proof_lines: The catalytic efficiency of YggF is 3-fold lower than that of GlpX, the other FBPase class 2 in E.coli.

substrate: fructose 1,6-bisphosphate


proof_lines: The kinetic constants are determined for the recombinant enzyme expressed in E.coli.


substrate_name: fructose 1,6-biphosphate

substrate: fructose 1,6-biphosphate


organism: Rhodococcus opacus

substrate_name: sedoheptulose 1,7-diphosphate

substrate: sedoheptulose 1,7-diphosphate


organism: Archaeoglobus fulgidus


organism: Bacillus methanolicus


organism: Bacillus subtilis

proof_lines: in presence of 0.01 mM phosphoenolpyruvate


organism: Blastocladiella emersonii


organism: Bombus atratus


organism: Bombus terrestris

proof_lines: activated by Mg2+, at 22°C or activated by Mn2+ at 17°C


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

proof_lines: kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius) and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).

substrate: inositol-1-phosphate (at 85 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


substrate_name: 3'-phosphoadenosine 5'-phosphate (at pH 9.0 and 30 degrees Celsius)

proof_lines: The second-order rate constant for PAP was determined to be over 3 orders of magnitude greater than those determined for IMP and FBP.


substrate_name: p-nitrophenyl phosphate (at pH 5.5 and 37 degrees Celsius)

proof_lines: kcat is 0.00071 sec(-1) for phosphoglycerate mutase activity (PubMed:16672613). The enzyme's FBPase activity does not follow Michaelis-Menten kinetics but follows allosteric sigmoidal kinetics that show lower affinity for FBP compared with


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 80 degrees Celsius)

proof_lines: kcat is 2.5 sec(-1) for the FBPase activity (at 80 degrees Celsius) (PubMed:15274916). kcat is 0.62 sec(-1) for the FBPase activity (at 48 degrees Celsius). kcat is 0.91 sec(-1) for the FBP aldolase activity in the anabolic direction (at 48


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 95 degrees Celsius)

proof_lines: kcat is 17 sec(-1) for the FBPase activity (at 95 degrees Celsius). kcat is 7 sec(-1) for the FBPase activity (at 85 degrees Celsius). kcat is 2.9 sec(-1) for the FBPase activity (at 37 degrees Celsius).


organism: Bos taurus

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

proof_lines:
pH 7.5, lung
pH 7.5, lung enzyme in presence of AMP


organism: Campylobacter jejuni serotype O:2

substrate_name: D-fructose 1,6-bisphosphate


organism: Candidatus Cenarchaeum symbiosum

proof_lines: pH not specified in the publication, 40°C


organism: Citrus x paradisi


organism: Clonorchis sinensis


organism: Corynebacterium glutamicum


organism: Cyberlindnera jadinii


organism: Escherichia coli


proof_lines: 22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+


organism: Homo sapiens


mutation_signature: Δ4

mutation_type: deletion


proof_lines: liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C


mutation_signature: Δ6


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: fructose 1,6-bisphosphate (at 85 degrees Celsius)


organism: Sus scrofa

column_label: Table I row KmF16P2 (uM); column Wild type; substrate fructose 1,6-bisphosphate/F16P2.

raw_value_unit_evidence: Table I row KmF16P2 (uM), column Wild type: 1.2 +/- 0.05 uM.

row_label: KmF16P2 (uM)

table_label: Table I. Kinetic parameters for wild-type and Leu54 FBPases


organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

substrate_name: fructose-1,6-bisphosphate (at pH 8)

substrate: fructose-1,6-bisphosphate (at pH 8)


substrate_name: fructose 1,6-bisphosphate (at pH 8)

substrate: fructose 1,6-bisphosphate (at pH 8)


proof_lines:
wild-type
pH 9.0, 37°C, wild-type
wild-type, 22°C, pH 7.5


organism: Francisella tularensis

proof_lines: recombinant mutant T89S, pH and temperature not specified in the publication


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


organism: Gallus gallus


organism: Lactobacillus delbrueckii subsp. lactis

substrate_name: beta-D-glucose 1,6-bisphosphate

proof_lines: wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C

substrate: beta-D-glucose 1,6-bisphosphate


proof_lines: mutant enzyme K76A, in 50 mM K+HEPES pH 7.0 at 25°C


proof_lines: mutant enzyme H20N, in 50 mM K+HEPES pH 7.0 at 25°C


organism: Lathyrus oleraceus


proof_lines: pH 8.0, 26-27°C, recombinant nontreated mutant C173S/C178S

proof_lines: pH 8.0, 26-27°C, recombinant S-nitrosoglutathione-treated mutant C173S/C178S


proof_lines:
pH 6.6, 25°C, native enzyme
pH 6.6, 25°C, Trombin treated enzyme
pH 6.6, 25°C, recombinant enzyme


organism: Leishmania major


organism: Malus domestica

substrate_name: D-Fructose 1,6-bisphosphate; H2O


organism: Methanocaldococcus jannaschii

proof_lines: pH and temperature not specified in the publication


organism: Mus musculus

substrate_name: fructose 1,6-diphosphate


mutation_signature: Δ8


proof_lines: liver enzyme mutant M177T/C179Q, pH 7.5, 37°C


mutation_signature: Δ5


proof_lines: muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C


proof_lines: mutant Y57W, pH 7.0, 37°C, Hill-coefficient 2.0

proof_lines: mutant Y57W, pH 7.0, 37°C, Hill-coefficient 1.84


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme K274L


organism: Mustela vison

substrate_name: H2O; Fructose 1,6-bisphosphate


organism: Mycobacterium tuberculosis


proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


organism: Mycolicibacterium smegmatis

substrate_name: D-fructose 1,6-diphosphate

substrate: D-fructose 1,6-diphosphate


organism: Neisseria meningitidis


organism: Pisum sativum


organism: Ptyas dhumnades

proof_lines:
pH 7.5, 30°C, recombinant enzyme
pH 7.5, 30°C, chimeric enzyme


organism: Pyrobaculum calidifontis

proof_lines:
recombinant enzyme, pH 8.0, 55°C
pH 8.0, 25°C


organism: Pyrococcus furiosus


organism: Rattus norvegicus

substrate_name: H2O; D-Fructose 1,6-bisphosphate


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: D-fructose 1,6-bisphosphate (at 85 degrees Celsius)

proof_lines: kcat is 23.4 sec(-1) for FBPase activity (at 85 degrees Celsius). FBPase activity is 5-fold higher than the IMPase activity.


organism: Thermococcus onnurineus (strain NA1)

substrate_name: FBP

proof_lines: kcat is 14.84 sec(-1) for the FBPase activity (at 95 degrees Celsius).

substrate: FBP


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: DL-inositol-1-phosphate (at 95 degrees Celsius)

proof_lines: kcat is 207 sec(-1) for IMPase activity (at 95 degrees Celsius) and 268 sec(-1) for FBPase activity (at 95 degrees Celsius).


organism: Bacillus subtilis (strain 168)

substrate_name: fructose 1,6-bisphosphate


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


organism: Escherichia coli (strain K12)

substrate_name: fructose 1,6-biphosphate


organism: Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius)


organism: Oryctolagus cuniculus


organism: Saccharomyces cerevisiae

substrate: D-fructose 1,6-bisphosphate


proof_lines:
at 10 mM Mg2+
at 2 mM Mg2+


organism: Salmonella enterica

substrate_name: Unknown

proof_lines: mutant enzyme G20S, uncompetitive dissociation constant Kiu

proof_lines: mutant enzyme G20S, competitive dissociation constant Kic

substrate: Unknown


organism: Spinacia oleracea


organism: Sulfurisphaera tokodaii

substrate_name: D-fructose 1,6-bisphosphate


organism: Sus scrofa


organism: Rhodopseudomonas palustris

substrate_name: sedoheptulose 1,7-diphosphate


organism: Ricinus communis


organism: Ogataea angusta

proof_lines:
enzyme from ethanol-grown cells
enzyme from methanol-grown cells


proof_lines:
native rabbit muscle FBPase
in presence of 5 mM Mg2+
in presence of 5 mM Mn2+


organism: Oryza coarctata


organism: Oryza sativa


organism: Pelophylax lessonae

proof_lines:
pH 7.5, 25°C, in presence of 500 nM AMP
pH 7.5, 25°C, in presence of 50 nM AMP
pH 7.5, 25°C


organism: Salmo salar

substrate: H2O; D-Fructose 1,6-bisphosphate


proof_lines: mutant enzyme T19I, competitive dissociation constant Kic

proof_lines: mutant enzyme T19I, uncompetitive dissociation constant Kiu


proof_lines: mutant enzyme T23I, competitive dissociation constant Kic

proof_lines: mutant enzyme T23I, uncompetitive dissociation constant Kiu


proof_lines: wild-type enzyme, competitive dissociation constant Kic

proof_lines: wild-type enzym, uncompetitive dissociation constant Kiu


organism: Sus scrofa domesticus

proof_lines:
pH 7.5, lung
pH 7.5, lung enzyme in presence of AMP
pH 7.5, lung enzyme


organism: Synechocystis sp.

proof_lines: wild-type, Hill coefficient 1.9, pH 8.0, 28°C


proof_lines: mutant D198H, Hill coefficient 1.9, pH 8.0, 28°C


proof_lines: mutant K134A, Hill coefficient 2.2, pH 8.0, 28°C


proof_lines: mutant T102A, Hill coefficient 2.5, pH 8.0, 28°C


proof_lines: mutant D200A, Hill coefficient 1.4, pH 8.0, 28°C


proof_lines: 30°C, pH 7.5, recombinant wild-type enzyme


proof_lines:
30°C, pH 7.5, nonrecombinant enzyme
pH 7.5, 30°C


organism: Trachemys scripta elegans

proof_lines:
enzyme from healthy liver, pH 7.2, 22°C
enzyme from anoxic liver, pH 7.2, 22°C


organism: Triticum aestivum

proof_lines: pH 8.8, 25°C, the recombinant enzyme in presence of 2 mM Mg2+

proof_lines: pH 8.8, 25°C, the recombinant enzyme in presence of 10 mM Mg2+


organism: Vigna radiata


organism: Yarrowia lipolytica


proof_lines: mutant N213A, Hill coefficient 1.8, pH 8.0, 28°C


proof_lines: mutant R178A, Hill coefficient 1.1, pH 8.0, 28°C


proof_lines: mutant R176A, Hill coefficient 1.2, pH 8.0, 28°C


proof_lines: mutant F309A, Hill coefficient 1.8, pH 8.0, 28°C


organism: Thermococcus kodakarensis


organism: Thermotoga maritima

proof_lines: pH 7.5, 60°C, purified recombinant enzyme

proof_lines: pH 7.5, 80°C, purified recombinant enzyme


proof_lines: mutant R307A, Hill coefficient 1.6, pH 8.0, 28°C


proof_lines: mutant Y131A, Hill coefficient 1.6, pH 8.0, 28°C


proof_lines: mutant R314A, Hill coefficient 1.8, pH 8.0, 28°C


proof_lines: mutant K29A, Hill coefficient 2.0, pH 8.0, 28°C


proof_lines: mutant H215A, Hill coefficient 1.4, pH 8.0, 28°C


proof_lines: mutant R164A, Hill coefficient 2.1, pH 8.0, 28°C


organism: Homo sapiens

mutation_signature: Δ3


mutation_signature: Δ7


proof_lines: muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C


organism: Lactobacillus delbrueckii subsp. lactis

proof_lines: mutant enzyme H20A, in 50 mM K+HEPES pH 7.0 at 25°C


proof_lines: mutant enzyme T16P, in 50 mM K+HEPES pH 7.0 at 25°C


proof_lines: mutant enzyme H20Q, in 50 mM K+HEPES pH 7.0 at 25°C


enzyme_display_name: beta-lactamase

organism: Kluyvera ascorbata

substrate_name: Imipenem

assay_conditions_summary: pH 7; 298.15 K; buffer Km context

proof_lines: Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C

enzyme: beta-lactamase

substrate: Imipenem


enzyme_display_name: fructose-bisphosphate aldolase

organism: Anoxybacillus gonensis

assay_conditions_summary: pH 8.5; 333.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer at pH 8.5 and 60°C

enzyme: fructose-bisphosphate aldolase


organism: Archaeoglobus fulgidus

proof_lines: 50°C, pH not specified in the publication


organism: Ascaris suum


organism: Bacillus cereus

proof_lines:
in Tris-HCl pH 8.0, at 30°C
pH 7.3, 28°C


organism: Bacillus methanolicus

substrate_name: glycerone phosphate

substrate: glycerone phosphate


organism: Bacillus subtilis


organism: Bos taurus

substrate_name: D-Fructose 1,6-bisphosphate

substrate: D-Fructose 1,6-bisphosphate


organism: Bubalus bubalis


organism: Callospermophilus lateralis


organism: Candida albicans

proof_lines: pH and temperature not specified in the publication, mutant enzyme T290A


proof_lines: pH and temperature not specified in the publication, mutant enzyme D289A


assay_conditions_summary: pH 7.4; 303.15 K; buffer and pH/temperature only

proof_lines: in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication


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


proof_lines: pH and temperature not specified in the publication, mutant enzyme S62A


proof_lines: pH and temperature not specified in the publication, mutant enzyme R332A


organism: Candidatus Cenarchaeum symbiosum


organism: Ceratitis capitata


organism: Chara foetida


organism: Chara vulgaris

proof_lines:
enzyme form I
enzyme form II


organism: Escherichia coli


proof_lines:
30°C, wild-type enzyme
wild-type enzyme, 30°C


organism: Giardia duodenalis

proof_lines: mutant enzyme R259A/D278A, at pH 8.0 and 37°C


proof_lines: at pH 7.5 and 25°C, in the absence of Zn2+


organism: Haloarcula vallismortis


organism: Haloferax mediterranei


organism: Haloferax volcanii


organism: Homo sapiens

substrate_name: D-Fructose 1-phosphate

substrate: D-Fructose 1-phosphate


proof_lines:
pH 7.4, 10°C, wild-type enzyme
wild-type enzyme, 22°C
pH 7.4, 30°C, wild-type enzyme


proof_lines:
W147R mutant, 22°C
W147R, 22°C, pH 7.6


organism: Euglena gracilis

proof_lines:
aldolase I
aldolase II


organism: Galdieria sulphuraria

proof_lines:
plastidic enzyme
cytosolic enzyme


organism: Gallus gallus


proof_lines: wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25°C


proof_lines: mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25°C


organism: Cyprinus carpio


organism: Daucus carota


organism: Echinococcus multilocularis


organism: Edwardsiella ictaluri


organism: Entamoeba histolytica

mutation_signature: but it still stops at enzyme-family and substrate context. Without a resolved accession or variant sequence

mutation_type: truncation


organism: Epiblema scudderiana


organism: Lethenteron camtschaticum

substrate_name: fructose 1-phosphate

proof_lines:
muscle-type enzyme
recombinant muscle-type enzyme
non-muscle-type enzyme

substrate: fructose 1-phosphate


organism: Methanocaldococcus jannaschii


organism: Methylococcus capsulatus

substrate_name: dihydroxyacetone phosphate

proof_lines: in the presence of 0.02 mM Co2+, at substrate concentrations of 0.008-0.5 mM, at pH 7.5, 30°C

proof_lines: in the presence of 0.02 mM Co2+, at substrate concentrations of 0.5-1.5 mM, at pH 7.5, 30°C

substrate: dihydroxyacetone phosphate


organism: Micrococcus aerogenes


organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.3; 301.15 K; buffer glycyl-glycine

proof_lines: purified C-His-rMtFBA, indicates that the extra five histidine residues in C-His-rMtFBA has negligible effects on the kinetic properties of the enzyme


organism: Mycolicibacterium smegmatis


organism: Helicobacter pylori


organism: Helix pomatia


organism: Homo sapiens

proof_lines: pH 7.4, 30°C, enzyme from patients with intolerance

proof_lines: pH 7.4, 10°C, enzyme from patients with intolerance


organism: Oryctolagus cuniculus


proof_lines:
mutant enzyme E187Q
E187Q mutant, pH 7.6, 22°C


proof_lines:
wild type enzyme, at pH 8.0 and 25°C
native wild type enzyme
wild-type enzyme


proof_lines:
mutant enzyme E187A
E187A mutant, pH 7.6, 22°C


proof_lines: turnover number less than 0.0002 sec-1, mutant enzyme K146A


proof_lines:
L256P mutant, 22°C
L256P, 22°C, pH 7.6


organism: Lactococcus lactis subsp. lactis


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Lac- Gal d


organism: Lathyrus oleraceus

proof_lines:
cytosolic enzyme
chloroplastic enzyme
cytoplasmic enzyme


organism: Leishmania mexicana


organism: Pagrus major


organism: Phaseolus vulgaris


organism: Pseudomonas aeruginosa

proof_lines:
in Tris-HCl pH 8.0, at 30°C
pH 7.3, 28°C


organism: Pseudomonas putida


organism: Pyricularia grisea

proof_lines:
in Tris-HCl pH 8.0, at 30°C
at pH 7.8
pH 7.3, 28°C


organism: Pyrobaculum calidifontis

proof_lines:
pH 8.0, 25°C
at pH 6.0 and 25°C
recombinant enzyme, pH 8.0, 55°C


organism: Halothece sp. PCC 7418


assay_conditions_summary: pH 7.4; buffer glycyl-glycine

proof_lines: in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication


proof_lines: kcat less than 0.00002 1/sec, mutant enzyme D82N, at pH 7.4 and 25°C


organism: Trachemys scripta elegans

proof_lines: pH 7.2, 25°C, normoxic liver preparation


organism: Triticum aestivum

proof_lines:
cytosolic enzyme
chloroplastic enzyme


organism: Trypanosoma brucei


organism: Ustilago maydis


organism: Vigna radiata


organism: Yersinia pestis


organism: Zea mays


organism: Spermophilus lateralis


organism: Spinacia oleracea


organism: Staphylococcus aureus


organism: Staphylococcus carnosus

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

proof_lines: native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C

proof_lines: recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C


organism: Sulfurisphaera tokodaii


organism: Sus scrofa


organism: Synechococcus elongatus PCC 7942 = FACHB-805


organism: Synechocystis sp.

proof_lines: pH 8, class I aldolase, recombinant enzyme

proof_lines: pH 7.5, class II aldolase, purified enzyme

proof_lines: pH 7.5, class II aldolase, recombinant enzyme


organism: Thermoproteus tenax

substrate: fructose 1,6-bisphosphate


organism: Thermus aquaticus


organism: Toxoplasma gondii

proof_lines:
at pH 7.5 and 25°C
pH 7.5, 25°C


organism: Pyrococcus furiosus


organism: Rattus norvegicus


organism: Ricinus communis


organism: Saccharolobus solfataricus

substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Saccharomyces cerevisiae

substrate_name: beta-D-Fructose 1,6-bisphosphate

substrate: beta-D-Fructose 1,6-bisphosphate


organism: Scomber japonicus


organism: Mycoplasmopsis bovis


organism: Neisseria meningitidis

proof_lines: at 30°C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0)


organism: Nocardia asteroides


organism: Oryctolagus cuniculus

assay_conditions_summary: pH 9.3; 303.15 K; buffer glycyl-glycine


enzyme_display_name: phosphoglycerate kinase

organism: Bos taurus

substrate_name: ATP; 3-Phospho-D-glycerate

assay_conditions_summary: cofactor ATP

enzyme: phosphoglycerate kinase

substrate: ATP; 3-Phospho-D-glycerate


organism: Chlamydomonas reinhardtii


substrate_name: ATP

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ATP

substrate: ATP


organism: Entamoeba histolytica

substrate_name: 3-Phospho-D-glycerate; ATP

substrate: 3-Phospho-D-glycerate; ATP


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Equus caballus


organism: Escherichia coli


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: dCTP

substrate: dCTP


substrate_name: dTTP

substrate: dTTP


substrate_name: CTP

substrate: CTP


substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

substrate: ADP


substrate_name: ddCTP

substrate: ddCTP


substrate_name: TDP

substrate: TDP


substrate_name: dADP

substrate: dADP


substrate_name: Glycerate 1,3-bisphosphate; ADP

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant K220A

substrate: Glycerate 1,3-bisphosphate; ADP


substrate_name: dATP

substrate: dATP


substrate_name: ADP; Glycerate 1,3-bisphosphate

assay_conditions_summary: cofactor ADP

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant E344A

substrate: ADP; Glycerate 1,3-bisphosphate


substrate_name: Glycerate 3-phosphate; ATP

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant PGK1 G157V

substrate: Glycerate 3-phosphate; ATP


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant C315R


organism: Fasciola hepatica


organism: Gallus gallus

sequence_source: UniProt REST canonical sequence for P51903


organism: Geobacillus stearothermophilus

substrate_name: ATP; Glycerate 3-phosphate

sequence_source: UniProt REST canonical sequence for P18912

substrate: ATP; Glycerate 3-phosphate


sequence_source: UniProt REST canonical sequence for P00558

column_label: Captured JBC full-text kinetic table index 1 (nucleoside diphosphate substrates; column headers Km in micromolar and kcat in s^-1); row dADP; wild type PGK; column Km (uM) cell 488.1; column kcat (s^-1) cell 844.5; no absolute kcat/Km column is printed in this table.

normalized_value_unit_evidence: kcat 844.5 s^-1 is already in s^-1, so paper kcat = 844.5 s^-1. Km 488.1 uM = 488.1/1000 = 0.4881 mM, which is 0.488 mM at the exported three-decimal mM precision. The table prints no absolute kcat/Km column, so paper kcat/Km = paper kcat / paper Km = 844.5 / 0.488 = 1730.532786885246 s^-1 mM^-1. Exported values reproduced: kcat 844.5 s^-1; Km 0.488 mM; kcat/Km 1730.532786885246 s^-1 mM^-1.

raw_value_unit_evidence: Captured JBC full-text kinetic table index 1 (nucleoside diphosphate substrates; column headers Km in micromolar and kcat in s^-1), row dADP; wild type PGK: Km column 488.1 +/- 12.5 uM; kcat column 844.5 +/- 230.4 s^-1.

row_label: dADP; wild type PGK


column_label: Captured JBC full-text kinetic table index 1 (nucleoside diphosphate substrates; column headers Km in micromolar and kcat in s^-1); row TDP; wild type PGK; column Km (uM) cell 160.5; column kcat (s^-1) cell 0.3; no absolute kcat/Km column is printed in this table.

normalized_value_unit_evidence: kcat 0.3 s^-1 is already in s^-1, so paper kcat = 0.3 s^-1. Km 160.5 uM = 160.5/1000 = 0.1605 mM, which is 0.161 mM at the exported three-decimal mM precision. The table prints no absolute kcat/Km column, so paper kcat/Km = paper kcat / paper Km = 0.3 / 0.161 = 1.8633540372670807 s^-1 mM^-1. Exported values reproduced: kcat 0.3 s^-1; Km 0.161 mM; kcat/Km 1.8633540372670807 s^-1 mM^-1.

raw_value_unit_evidence: Captured JBC full-text kinetic table index 1 (nucleoside diphosphate substrates; column headers Km in micromolar and kcat in s^-1), row TDP; wild type PGK: Km column 160.5 +/- 13.4 uM; kcat column 0.3 +/- 0.003 s^-1.

row_label: TDP; wild type PGK


organism: Mus musculus


organism: Nitrosospira sp.


organism: Nitrosovibrio sp.


organism: Pseudomonas sp.


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558 reconstructed from K220R and applied mutation signature K220R to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical sequence for P00558 reconstructed from K220R


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558 reconstructed from N337D and applied mutation signature N337D to reconstruct the assayed variant sequence.


column_label: Captured JBC full-text kinetic table index 2 (nucleoside triphosphate substrates; column headers Km in micromolar and kcat in min^-1); row ATP; wild type PGK; column Km (uM) cell 58.8; column kcat (min^-1) cell 0.9; no absolute kcat/Km column is printed in this table.

normalized_value_unit_evidence: kcat 0.9 min^-1 = 0.9/60 = 0.015 s^-1. Km 58.8 uM = 58.8/1000 = 0.0588 mM, which is 0.059 mM at the exported three-decimal mM precision. The table prints no absolute kcat/Km column, so paper kcat/Km = paper kcat / paper Km = 0.015 / 0.059 = 0.2542372881355932 s^-1 mM^-1. Exported values reproduced: kcat 0.015 s^-1; Km 0.059 mM; kcat/Km 0.2542372881355932 s^-1 mM^-1.

raw_value_unit_evidence: Captured JBC full-text kinetic table index 2 (nucleoside triphosphate substrates; column headers Km in micromolar and kcat in min^-1), row ATP; wild type PGK: Km column 58.8 +/- 11.5 uM; kcat column 0.9 +/- 0.13 min^-1.

row_label: ATP; wild type PGK


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558 reconstructed from N337Q and applied mutation signature N337Q to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical sequence for P00558 reconstructed from N337Q


sequence_source: UniProt REST canonical sequence for P00558 reconstructed from N337D

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant N337D


column_label: Captured JBC full-text kinetic table index 2 (nucleoside triphosphate substrates; column headers Km in micromolar and kcat in min^-1); row dCTP; wild type PGK; column Km (uM) cell 109.8; column kcat (min^-1) cell 0.4; no absolute kcat/Km column is printed in this table.

normalized_value_unit_evidence: kcat 0.4 min^-1 = 0.4/60 = 0.006666666666666667 s^-1, which is 0.007 s^-1 at the exported three-decimal s^-1 precision. Km 109.8 uM = 109.8/1000 = 0.1098 mM, which is 0.11 mM at the exported three-decimal mM precision. The table prints no absolute kcat/Km column, so paper kcat/Km = paper kcat / paper Km = 0.007 / 0.11 = 0.06363636363636364 s^-1 mM^-1. Exported values reproduced: kcat 0.007 s^-1; Km 0.11 mM; kcat/Km 0.06363636363636364 s^-1 mM^-1.

raw_value_unit_evidence: Captured JBC full-text kinetic table index 2 (nucleoside triphosphate substrates; column headers Km in micromolar and kcat in min^-1), row dCTP; wild type PGK: Km column 109.8 +/- 3.9 uM; kcat column 0.4 +/- 0.04 min^-1.

row_label: dCTP; wild type PGK


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558; variant reconstructed from mutation signature K220R and applied mutation signature K220R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant K220R


column_label: Captured JBC full-text kinetic table index 2 (nucleoside triphosphate substrates; column headers Km in micromolar and kcat in min^-1); row CTP; wild type PGK; column Km (uM) cell 86.7; column kcat (min^-1) cell 0.5; no absolute kcat/Km column is printed in this table.

normalized_value_unit_evidence: kcat 0.5 min^-1 = 0.5/60 = 0.008333333333333333 s^-1, which is 0.008 s^-1 at the exported three-decimal s^-1 precision. Km 86.7 uM = 86.7/1000 = 0.0867 mM, which is 0.087 mM at the exported three-decimal mM precision. The table prints no absolute kcat/Km column, so paper kcat/Km = paper kcat / paper Km = 0.008 / 0.087 = 0.09195402298850576 s^-1 mM^-1. Exported values reproduced: kcat 0.008 s^-1; Km 0.087 mM; kcat/Km 0.09195402298850576 s^-1 mM^-1.

raw_value_unit_evidence: Captured JBC full-text kinetic table index 2 (nucleoside triphosphate substrates; column headers Km in micromolar and kcat in min^-1), row CTP; wild type PGK: Km column 86.7 +/- 1.7 uM; kcat column 0.5 +/- 0.09 min^-1.

row_label: CTP; wild type PGK


sequence_source: UniProt REST canonical sequence for P00558; variant reconstructed from mutation signature K220R


substrate_name: CDP

column_label: JBC HTML wild-type diphosphate substrate kinetic table; row CDP; wild type PGK; column Km (uM) raw 885.0; column kcat (s^-1) raw 0.9; no kcat/Km column printed, value derived by division.

normalized_value_unit_evidence: Km 885.0 uM / 1000 = 0.885 mM. kcat 0.9 s^-1 = 0.9 s^-1 (already canonical, no conversion). kcat/Km is not printed in this table; derived as paper kcat / paper Km = 0.9 / 0.885 = 1.0169491525423728 s^-1 mM^-1, which equals the catalog value 1.0169491525423728 exactly.

raw_value_unit_evidence: JBC HTML wild-type diphosphate substrate kinetic table, row CDP; wild type PGK: Km = 885.0 +/- 11.0 uM; kcat = 0.9 +/- 0.1 s^-1. No kcat/Km column is printed for this table.

row_label: CDP; wild type PGK

substrate: CDP


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558; variant reconstructed from mutation signature N337Q and applied mutation signature N337Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant N337Q


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558; variant reconstructed from mutation signature K220A and applied mutation signature K220A to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

assay_conditions_summary: pH 6.9; 303.15 K; cofactor ADP


organism: Saccharomyces cerevisiae

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Pro204His


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Pro204Phe


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R38A


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant H62A


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R21M


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R21K


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant H388Q


substrate_name: Glycerate 3-phosphate

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

substrate: Glycerate 3-phosphate


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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5


organism: Pyrococcus woesei


substrate_name: ATP; 3-Phospho-D-glycerate

substrate: ATP; 3-Phospho-D-glycerate


substrate_name: ATP

assay_conditions_summary: pH 7.3; 303.15 K; buffer 27.8 mM iodoacetate in; cofactor NADH

column_label: Table II, backward direction, MgATP row: modified Vmax=0.22 mol min^-1 mL^-1, modified Km,app=0.91 mM, and modified Kcat=548 min^-1. Footnote a specifies the iodoacetate treatment/quench; footnote b defines Kcat and says modified [E] was determined from residual activity.

raw_value_unit_evidence: Table II, MgATP modified cells: Kcat 548 min^-1 and Km,app 0.91 mM. The table does not print a kcat/Km column; the package value is the quotient of the source-normalized, three-decimal kcat (9.133 s^-1) and the same modified-column Km (0.91 mM).

row_label: backward direction; MgATP; modified

table_label: Table II. Kinetic Constants of Native and Iodoacetate-Modified Phosphoglycerate Kinase

substrate: ATP


substrate_name: 3-Phospho-D-glyceroyl phosphate

substrate: 3-Phospho-D-glyceroyl phosphate


substrate_name: 3-Phospho-D-glycerate; ATP

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R121K

substrate: 3-Phospho-D-glycerate; ATP


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R121M


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R65M


assay_conditions_summary: pH 7.5; 277.15 K; cofactor ATP


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant K215A


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558; variant reconstructed from R38M on P00558 and applied mutation signature R38M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 355.15 K; cofactor NADH

column_label: PMID 29995887 Table 1 row R38M; columns KM (mM), kcat (s^-1), and kcat/KM (s^-1 mM^-1).

table_label: Table 1. Kinetic parameters of PGK1 wild type and variants

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558; variant reconstructed from G166D on P00558 and applied mutation signature G166D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PMID 29995887 Table 1 row G166D; columns KM (mM), kcat (s^-1), and kcat/KM (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row G166D: KM 1.54 mM; kcat 5.9 s^-1; kcat/KM 3.8 s^-1 mM^-1.


column_label: PMID 29995887 Table 1 row Wild type; columns KM (mM), kcat (s^-1), and kcat/KM (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row Wild type: KM 0.40 mM; kcat 89.8 s^-1; kcat/KM 224.5 s^-1 mM^-1.

row_label: Wild type


sequence_source: UniProt REST canonical sequence for P00558; variant reconstructed from V216F on P00558

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 canonical sequence from UniProt REST canonical sequence for P00558; variant reconstructed from R65W on P00558 and applied mutation signature R65W with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical sequence for P00558; variant reconstructed from F241S on P00558


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P00558 reconstructed from V266M and applied mutation signature V266M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Val266Met (PGKase-Tokyo)


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant PGK Creteil

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant PGK-Uppsala

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant PGK Alberta (myopathic)


organism: Homo sapiens P00558 GenBank


organism: Methanothermus fervidus


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Glu190Asp


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant His388Ala


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant His388Lys


substrate_name: 2-Hydroxy-4-phosphonobutyric acid

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

substrate: 2-Hydroxy-4-phosphonobutyric acid


sequence_source: UniProt REST canonical sequence for P00560


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R65K


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: recombinant enzyme, isoform PGKA, pH and temperature not specified in the publication


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

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

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


proof_lines: recombinant truncated isozyme PGKA mutant, pH 7.5, 22°C


organism: Monoraphidium minutum

assay_conditions_summary: pH 7.3; cofactor ATP

proof_lines:
isozyme PGK2, pH 7.3-7.8
ATP in form of MgATP2-
isozyme PGK1, pH 7.3


organism: Ustilago maydis


organism: Zymomonas mobilis


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines: recombinant cytosolic isozyme, pH 7.6, 25°C


proof_lines: recombinant truncated glycosomal isozyme, pH 7.6, 25°C


organism: Ovis aries

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: pH 7.5, isozyme PGKA, in presence of 0.05 mM 1,3-bisphosphoglycerate

proof_lines: pH 7.5, isozyme PGKB, in presence of 0.05 mM 1,3-bisphosphoglycerate


assay_conditions_summary: pH 6.9; 298.15 K; cofactor ATP

proof_lines:
isozyme PGK2C
isoenzyme PGK2C
pH 6.9, 25°C


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P00560 and applied mutation signature R121K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PDF page 4 / printed page 196, Table I, row R121K, columns Km 3-PGA, kcat, and kcat/Km; Table footnote supplies the 40 mM ammonium sulphate Km condition.

normalized_value_unit_evidence: For the 3-PGA tuple: kcat 232.1 s^-1; Km 1.92 mM; printed kcat/Km 120 s^-1 mM^-1.

raw_value_unit_evidence: Table I row R121K: Km 3-PGA 1.92 mM; Km MgATP 0.36 mM; kcat 232.1 s^-1; kcat/Km 1.2 x 10^5 s^-1 M^-1.

table_label: Table I: kinetic parameters for wild-type and site-directed mutant yeast PGK


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P00560 and applied mutation signature R65M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PDF page 4 / printed page 196, Table I, row R65M, columns Km MgATP and kcat; kcat/Km is the exact quotient of those two printed cells.

normalized_value_unit_evidence: For the ATP/MgATP tuple: kcat 48.9 s^-1; Km 1.62 mM; exact cell quotient kcat/Km 30.185185185185183 s^-1 mM^-1.

raw_value_unit_evidence: Table I row R65M: Km MgATP 1.62 mM and kcat 48.9 s^-1; requested kcat/Km is the exact quotient 48.9/1.62.

row_label: R65M / MgATP


column_label: PDF page 4 / printed page 196, Table I, row R65M, columns Km 3-PGA, kcat, and kcat/Km; Table footnote supplies the 40 mM ammonium sulphate Km condition.

normalized_value_unit_evidence: For the 3-PGA tuple: kcat 48.9 s^-1; Km 15.89 mM; printed kcat/Km 3.1 s^-1 mM^-1.

row_label: R65M / 3-PGA


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P00560 and applied mutation signature R168K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PDF page 4 / printed page 196, Table I, row R168K, columns Km MgATP and kcat; kcat/Km is the exact quotient of those two printed cells.

normalized_value_unit_evidence: For the ATP/MgATP tuple: kcat 164.1 s^-1; Km 0.99 mM; exact cell quotient kcat/Km 165.75757575757575 s^-1 mM^-1.

raw_value_unit_evidence: Table I row R168K: Km MgATP 0.99 mM and kcat 164.1 s^-1; requested kcat/Km is the exact quotient 164.1/0.99.

row_label: R168K / MgATP


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P00560 and applied mutation signature R65K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PDF page 4 / printed page 196, Table I, row R65K, columns Km 3-PGA, kcat, and kcat/Km; Table footnote supplies the 40 mM ammonium sulphate Km condition.

normalized_value_unit_evidence: For the 3-PGA tuple: kcat 503.8 s^-1; Km 1.70 mM; printed kcat/Km 300 s^-1 mM^-1.

row_label: R65K / 3-PGA


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P00560 and applied mutation signature R168M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PDF page 4 / printed page 196, Table I, row R168M, columns Km MgATP and kcat; kcat/Km is the exact quotient of those two printed cells.

normalized_value_unit_evidence: For the ATP/MgATP tuple: kcat 85.5 s^-1; Km 1.34 mM; exact cell quotient kcat/Km 63.805970149253724 s^-1 mM^-1.

raw_value_unit_evidence: Table I row R168M: Km MgATP 1.34 mM and kcat 85.5 s^-1; requested kcat/Km is the exact quotient 85.5/1.34.

row_label: R168M / MgATP


column_label: PDF page 4 / printed page 196, Table I, row R168K, columns Km 3-PGA, kcat, and kcat/Km; Table footnote supplies the 40 mM ammonium sulphate Km condition.

normalized_value_unit_evidence: For the 3-PGA tuple: kcat 164.1 s^-1; Km 2.01 mM; printed kcat/Km 82 s^-1 mM^-1.


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


organism: Abramis brama

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


organism: Acidovorax facilis


organism: Arthrospira platensis


organism: Beta vulgaris

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines:
pH 7.5, 30°C
ATP in form of MgATP2-


organism: Brugia malayi

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP


organism: Chlamydomonas reinhardtii

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ATP

proof_lines: pH 7.9, 25°C, recombinant oxidized wild-type enzyme

proof_lines: pH 7.9, 25°C, recombinant reduced wild-type enzyme


organism: Homo sapiens

assay_conditions_summary: cofactor ATP


organism: Columba livia


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication

proof_lines: pH 7.4, 30°C, recombinant His-tagged enzyme


organism: Dromaius novae-hollandiae


organism: Entamoeba histolytica

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

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: recombinant purified mutant Y239F, at 37°C, pH 7.0


proof_lines: recombinant purified wild-type, at 37°C, pH 7.0

proof_lines: wild-type, in cytosolic-enriched cellular extracts, at 37°C, pH 7.0

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


proof_lines: recombinant purified mutant V311L, at 37°C, pH 7.0


proof_lines: recombinant purified mutant E309M, at 37°C, pH 7.0


proof_lines: recombinant purified mutant Y239F/E309M, at 37°C, pH 7.0


proof_lines: recombinant purified mutant E309Q, at 37°C, pH 7.0


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


organism: Equus caballus

substrate_name: Unknown

proof_lines:
versus MgATP2-
versus 3-phospho-D-glycerate

substrate: Unknown


organism: Escherichia coli


assay_conditions_summary: pH 7.5; 277.15 K; buffer methanol-free; cofactor ATP

proof_lines: mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+

proof_lines: mutant K215A, at 20°C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+


proof_lines: co-substrate: ATP, mutant D374A, pH and temperature not specified in the publication


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant 71BLA chimeric PGK/BLA

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant 89BLA chimeric PGK/BLA

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant 129BLA chimeric PGK/BLA


organism: Fasciola hepatica


organism: Geobacillus stearothermophilus

proof_lines: pH and temperature not specified in the publication


organism: Helianthus annuus

assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP


organism: Hippoglossus hippoglossus


organism: Hippoglossus stenolepis


proof_lines: co-substrate: ATP, mutant D218A, pH and temperature not specified in the publication


proof_lines: co-substrate: ATP, mutant D218A/D374A, pH and temperature not specified in the publication


organism: Spinacia oleracea


organism: Sulfolobus solfataricus

sequence_source: UniProt REST canonical sequence for P50317

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


organism: Sus scrofa


organism: Thermotoga maritima

sequence_source: UniProt REST canonical sequence for P36204


organism: Thermus thermophilus

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Trypanosoma brucei


organism: Trypanosoma brucei brucei


organism: Homo sapiens


organism: Lactobacillus delbrueckii subsp. lactis

assay_conditions_summary: pH 6.8; 318.15 K; cofactor ATP


organism: Lathyrus oleraceus

proof_lines:
pH 7.3
ATP in form of MgATP2-


organism: Leishmania major

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines:
mutant enzyme H71A, at pH 7.5 and 25°C
mutant enzyme H71A, at pH 5.5 and 25°C


organism: Saccharomyces cerevisiae

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R21A


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant H167S


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R168Q


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Arg168Met

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R168M


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Arg168Lys

proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant R168K


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant H62Q


proof_lines: SABIO-RK modifier species: phosphoglycerate kinase(Enzyme) mutant Glu190Gln


organism: Leishmania mexicana mexicana

proof_lines: isoform PGKB, pH and temperature not specified in the publication


organism: Lutjanus campechanus


organism: Macropus fuliginosus


organism: Macropus giganteus


organism: Methanothermus fervidus

assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP

proof_lines:
pH 7.5, 60°C, native enzyme
pH 7.5, 60°C, recombinant enzyme
pH 7.5, 70°C


organism: Nitrosolobus multiformis


assay_conditions_summary: pH 7.5; 310.15 K; buffer methanol-free; cofactor ATP

proof_lines: wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+

proof_lines: co-substrate: ATP, wild-type, pH and temperature not specified in the publication


proof_lines: pH 7.5, temperature not specified in the publication

proof_lines: at pH 7.4, temperature not specified in the publication


organism: Nitrosolobus sp.


organism: Nitrosospira multiformis ATCC 25196


organism: Nitrosospira sp.


organism: Nitrosospira sp. GS833


organism: Nitrosospira sp. KAN8


organism: Nitrosospira sp. NRS527


organism: Nitrosospira sp. PJA1


organism: Nitrosospira sp. TCH716


organism: Nitrosospira sp. TYM9


organism: Nitrosovibrio sp.


organism: Nitrosovibrio sp. FJI423


organism: Nitrosovibrio sp. FJI82


organism: Leishmania major

mutation_signature: truncated enzyme

assay_conditions_summary: pH 5.5; 298.15 K; cofactor ATP

proof_lines:
truncated enzyme, at pH 5.5 and 25°C
truncated enzyme, at pH 7.5 and 25°C


proof_lines: pH and temperature not specified in the publication


proof_lines:
mutant enzyme H89A, at pH 7.5 and 25°C
mutant enzyme H89A, at pH 5.5 and 25°C


proof_lines:
mutant enzyme H57A, at pH 5.5 and 25°C
mutant enzyme H57A, at pH 7.5 and 25°C


proof_lines:
wild type enzyme, at pH 7.5 and 25°C
wild type enzyme, at pH 5.5 and 25°C


proof_lines:
mutant enzyme H111A, at pH 7.5 and 25°C
mutant enzyme H111A, at pH 5.5 and 25°C


organism: Nitrosovibrio sp. RY3C


organism: Nitrosovibrio sp. RY6A


organism: Oncorhynchus mykiss


organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7; cofactor ATP


organism: Phaeodactylum tricornutum


organism: Plasmodium falciparum

substrate_name: ADP; 3-Phospho-D-glyceroyl phosphate

substrate: ADP; 3-Phospho-D-glyceroyl phosphate


organism: Pyrococcus woesei

assay_conditions_summary: pH 7.5; 343.15 K; cofactor ATP

proof_lines:
recombinant enzyme, 70°C
pH 7.5, 70°C, native enzyme
pH 7.5, 70°C, recombinant enzyme


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

proof_lines: heart and skeletal muscle enzymes, pH 7.4, 25°C


organism: Saccharolobus solfataricus

substrate_name: 3-phospho-D-glyceroyl phosphate

assay_conditions_summary: pH 7; 343.15 K; cofactor ADP

proof_lines:
at pH 7.0 and 70°C
70°C, pH 6.5
at pH 7.0 and 30°C

substrate: 3-phospho-D-glyceroyl phosphate


organism: Saccharomyces cerevisiae

substrate_name: 3-Phospho-D-glyceroyl phosphate; ADP

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP

substrate: 3-Phospho-D-glyceroyl phosphate; ADP


proof_lines: wild-type, in cytosolic-enriched cellular extracts, at 37°C, pH 7.0


organism: Trypanosoma brucei brucei

proof_lines: recombinant enzyme, isoform PGKC, pH and temperature not specified in the publication


organism: Trypanosoma rangeli

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


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

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


organism: Turbatrix aceti


organism: Vombatus ursinus


organism: Zymomonas mobilis

assay_conditions_summary: pH 6.5; 298.15 K; cofactor ATP


organism: Salmo trutta

assay_conditions_summary: cofactor ATP


organism: Spinacia oleracea


organism: Spirulina geitleri

proof_lines: at 1.5-13 mM 3-phospho-D-glycerate concentration


organism: Sus scrofa

proof_lines: pH 7.5, 20°C, versus 3-phospho-D-glycerate


organism: Synechocystis sp.

proof_lines: wild-type, 30°C, pH not specified in the publication


organism: Synechocystis sp. PCC 6803


organism: Pseudocheirus peregrinus


organism: Pseudomonas sp.

proof_lines: recombinant His-tagged enzyme, pH 7.5, 25°C


proof_lines: recombinant wild-type enzyme, pH 7.5, 25°C


organism: Pseudomonas sp. 'TAC II 18'


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

proof_lines: His-tagged recombinant enzyme, pH and temperature not specified in the publication


organism: Pyrococcus furiosus

proof_lines: 50°C, pH not specified in the publication


organism: Thermoanaerobacterium sp.


organism: Thermus thermophilus

proof_lines: pH and temperature not specified in the publication


organism: Thylogale billardieri


organism: Trichosurus vulpecula


organism: trout

proof_lines:
versus MgATP2-
versus 3-phospho-D-glycerate


organism: Trypanosoma brucei brucei

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

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


organism: Aeromonas hydrophila

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=9
Raw SKiD Env: Temp=30°C, pH=6.5


organism: Bacillus cereus

substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H196S

substrate: H2O; Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H116S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H263S


substrate_name: Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R

substrate: Nitrocefin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R, E166D


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P04190; reconstructed from D120E and applied mutation signature D120E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120E; fusion protein to glutathione-S-transferase


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical sequence for P04190; reconstructed from D120Q and applied mutation signature D120Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120Q; fusion protein to glutathione-S-transferase


organism: Mycobacterium tuberculosis


organism: Providencia stuartii

substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K104E

substrate: H2O; Nitrocefin


organism: Pseudomonas aeruginosa


substrate_name: Penicillin G; H2O

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N104G

substrate: Penicillin G; H2O


organism: Chryseobacterium indologenes

substrate_name: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)

assay_conditions_summary: pH 7


organism: Psychrobacter immobilis

substrate_name: ampicillin

assay_conditions_summary: pH 7; 303.15 K; buffer phosphate

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

substrate: ampicillin


organism: Kluyvera ascorbata

substrate_name: Imipenem

assay_conditions_summary: pH 7; 298.15 K; buffer and temperature conditions

proof_lines: Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C

substrate: Imipenem


organism: Shouchella clausii

substrate_name: cefoxitin

proof_lines: kcat less than 0.01/sec at 30°C in 100 mM sodium phosphate (pH 7)

proof_lines: kcat less than 0.3/sec at 30°C in 100 mM sodium phosphate (pH 7)

substrate: cefoxitin


enzyme_display_name: pyruvate kinase

organism: Homo sapiens

assay_conditions_summary: pH 8; 305.15 K; cofactor ADP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=32°C, pH=8
Raw SKiD Env: Temp=25°C, pH=6

enzyme: pyruvate kinase


organism: Lactococcus lactis subsp. cremoris

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


substrate_name: phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)

assay_conditions_summary: pH 8


substrate_name: phosphoenolpyruvate

proof_lines: mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C

substrate: phosphoenolpyruvate


organism: Lactococcus lactis subsp. lactis

substrate_name: Pyruvate; ATP

substrate: Pyruvate; ATP


organism: Leishmania mexicana

substrate_name: ADP

substrate: ADP


organism: Mucor rouxii

substrate_name: Phosphoenolpyruvate; ADP

substrate: Phosphoenolpyruvate; ADP


organism: Mus musculus


organism: Streptococcus sanguis


substrate_name: Cephalosporin C

substrate: Cephalosporin C


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166D


organism: Bacteroides fragilis

substrate_name: Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D103N CcrA3

substrate: Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H99N CcrA3


organism: Rattus norvegicus

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432D


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432D


organism: Corynebacterium glutamicum


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K382Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K382Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R431E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R431E


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K413Q to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T403K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R459Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K292Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T311M


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant E392A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R77Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298S


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R271L


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K413Q


organism: Staphylococcus aureus

substrate_name: H2O; Cephaloridine

substrate: H2O; Cephaloridine


enzyme_display_name: beta-galactosidase

organism: Arabidopsis thaliana

substrate_name: o-Nitrophenyl-beta-D-galactoside

enzyme: beta-galactosidase

substrate: o-Nitrophenyl-beta-D-galactoside


substrate_name: p-Nitrophenyl-beta-D-galactoside

substrate: p-Nitrophenyl-beta-D-galactoside


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

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


organism: Arthrobacter sp.

substrate_name: lactose

substrate: lactose


substrate_name: o-Nitrophenyl-beta-D-galactoside; H2O

substrate: o-Nitrophenyl-beta-D-galactoside; H2O


organism: Aspergillus niger

substrate_name: H2O; Lactose

substrate: H2O; Lactose


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304F/Y355H/N357G/W806F His6-tagged


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391E


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391F


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


organism: Bacteroides ovatus

sequence_source: UniProtKB reviewed entry A7LXS9

assay_conditions_summary: pH 6; 310.15 K; buffer and pH optimum

column_label: Extended Data Table ED1; row BoGH2A / Gal-beta-PNP; columns kcat (s^-1), Km (mM), and same-row kcat/Km quotient; raw kcat 4.0 +/- 0.092; raw Km 0.087 +/- 0.0074.

row_label: BoGH2A / Gal-beta-PNP

table_label: Extended Data Table ED1: Summary of kinetic analyses of XyGUL glycoside hydrolases


organism: Bifidobacterium bifidum


substrate_name: Lactose; H2O

substrate: Lactose; H2O


substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391K

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature W806F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 3.5; buffer citrate-phosphate

column_label: PMID 28391618 / DOI 10.1111/febs.14083, Wiley Table 2, column W806F, metric rows Kcat (s^-1) and Km (mM), lactose hydrolysis condition.

row_label: W806F / lactose hydrolysis

table_label: Table 2. Kinetic analysis of lactose hydrolysis by AnbGal variants and AobGal


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature W806S to reconstruct the assayed variant sequence.

column_label: PMID 28391618 / DOI 10.1111/febs.14083, Wiley Table 2, column W806S, metric rows Kcat (s^-1) and Km (mM), lactose hydrolysis condition.

row_label: W806S / lactose hydrolysis


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature Y304F/Y355H/N357G to reconstruct the assayed variant sequence.

column_label: PMID 28391618 / DOI 10.1111/febs.14083, Wiley Table 2, column Y304F/Y355H/N357G, metric rows Kcat (s^-1) and Km (mM), lactose hydrolysis condition.

row_label: Y304F/Y355H/N357G / lactose hydrolysis


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature Y304F to reconstruct the assayed variant sequence.

column_label: PMID 28391618 / DOI 10.1111/febs.14083, Wiley Table 2, column Y304F, metric rows Kcat (s^-1) and Km (mM), lactose hydrolysis condition.

row_label: Y304F / lactose hydrolysis


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature Y304A to reconstruct the assayed variant sequence.

column_label: PMID 28391618 / DOI 10.1111/febs.14083, Wiley Table 2, column Y304A, metric rows Kcat (s^-1) and Km (mM), lactose hydrolysis condition.

row_label: Y304A / lactose hydrolysis


organism: Aspergillus oryzae

proof_lines:
Raw SKiD Env: Temp=60°C, pH=4.5
Raw SKiD Env: Temp=60°C, pH=5


substrate_name: 2-nitrophenyl beta-D-galactoside

sequence_source: UniProtKB reviewed entry Q2UCU3 canonical wild-type sequence

substrate: 2-nitrophenyl beta-D-galactoside


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q2UCU3; reconstructed variant from W806F and applied mutation signature W806F to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999G


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999L


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999Y


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant G794A


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201E-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201N-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461Q


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461D


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461G


column_label: Table 2. Kinetic constants of LacA; row Lactose; columns Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1)

normalized_value_unit_evidence: kcat normalized_value=869 normalized_unit=s^-1 | km normalized_value=104 normalized_unit=mM | kcat_over_km normalized_value=8.36 normalized_unit=s^-1 mM^-1

row_label: Lactose

table_label: Table 2. Kinetic constants of LacA


substrate_name: 4-nitrophenyl beta-D-galactopyranoside

column_label: Table 2. Kinetic constants of LacA; row pNP beta-D-galactopyranoside; columns Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1)

normalized_value_unit_evidence: kcat normalized_value=525 normalized_unit=s^-1 | km normalized_value=1.42 normalized_unit=mM | kcat_over_km normalized_value=370 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Table 2 row pNP beta-D-galactopyranoside: Km = 1.42 +/- 0.08 mM; kcat = 525 +/- 8 s^-1; kcat/Km = 370 s^-1 mM^-1

row_label: pNP beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Bacillus coagulans


organism: Bacillus subtilis

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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E145A

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry O31529; reconstructed variant from E145A and applied mutation signature E145A 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.

assay_conditions_summary: buffer and pH optimum

column_label: Europe PMC JATS Table ED1, row BoGH2A / Gal-beta-PNP, columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1), Assay=PNP; methods define PNP assay and substrate list.

normalized_value_unit_evidence: kcat 4.0 s^-1; Km 0.087 mM; kcat/Km 46.0 s^-1*mM^-1. Exported ratio 45.97701149425288 equals 4.0/0.087 within table rounding.

raw_value_unit_evidence: Table ED1 row BoGH2A Gal-beta-PNP: kcat 4.0 +/- 0.092 s^-1; Km 0.087 +/- 0.0074 mM; kcat/Km 46.0 s^-1*mM^-1; assay PNP.


sequence_source: UniProtKB P00722

sequence_variant_note: Mutation signature E461H matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature E461G matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature E461D matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P06864


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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant psi epg0

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg a


substrate_name: Phenyl-beta-D-galactopyranoside

substrate: Phenyl-beta-D-galactopyranoside


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461H


column_label: Table I PNPA block; WILD column: kcat row 211, Km row 11.6, kcat/Km row 18.2.

normalized_value_unit_evidence: 211 s-1; 11.6 mM; kcat/Km reported 18.2 s-1 mM-1; 211/11.6 = 18.1897 s-1 mM-1 within table rounding.

raw_value_unit_evidence: PNPA WILD: kcat = 211 s-1; Km = 11.6 mM; kcat/Km = 18.2 s-1 mM-1.

row_label: PNPA row; WILD column; kcat, Km, kcat/Km subrows

table_label: PMID 8662937 Table I: kinetic and energetic values for wild type and substituted beta-galactosidases


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


substrate_name: p-Nitrophenyl-beta-D-fucopyranoside

column_label: PMID 8662937 Table I: kinetic and energetic values for wild type and substituted beta-galactosidases; row PNPF row; WILD column; kcat, Km, kcat/Km subrows

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

substrate: p-Nitrophenyl-beta-D-fucopyranoside


column_label: Table I PNPG block; WILD column: kcat row 90, Km row 0.041, kcat/Km row 2200; no row labeled p-nitrophenyl beta-D-galactopyranoside 6-phosphate.

normalized_value_unit_evidence: PNPG values would match the expected numbers within rounding, but the exact substrate label does not include 6-phosphate.

raw_value_unit_evidence: PNPG WILD row: kcat = 90 s-1; Km = 0.041 mM; kcat/Km = 2200 s-1 mM-1. No table row for p-nitrophenyl beta-D-galactopyranoside 6-phosphate was identified.

row_label: PNPG row; WILD column; no exact 6-phosphate row identified


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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540E


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357L


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357D


organism: Homo sapiens

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


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540F

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


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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540N


organism: Lactobacillus delbrueckii subsp. bulgaricus


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant L317F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant P429S


organism: Lactococcus lactis subsp. lactis


organism: Mus musculus


enzyme_display_name: Beta-galactosidase

organism: Sulfolobus solfataricus

column_label: Table 3 row Phenyl beta-D-galactopyranoside, columns Km=2.6 mM, kcat=166 min^-1, kcat/Km=63.8 min^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=2.6 normalized_unit=mM; kcat normalized_value=2.7666666666666666 normalized_unit=s^-1; kcat/Km normalized_value=1.0633333333333332 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=2.6 raw_unit=mM; kcat raw_value=166 raw_unit=min^-1; kcat/Km raw_value=63.8 raw_unit=min^-1*mM^-1

row_label: Phenyl beta-D-galactopyranoside

table_label: Table 3

enzyme: Beta-galactosidase


column_label: Table 3 row P-NpGal, columns Km=0.225 mM, kcat=5700 min^-1, kcat/Km=25333 min^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.225 normalized_unit=mM; kcat normalized_value=95 normalized_unit=s^-1; kcat/Km normalized_value=422.21666666666664 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.225 raw_unit=mM; kcat raw_value=5700 raw_unit=min^-1; kcat/Km raw_value=25333 raw_unit=min^-1*mM^-1

row_label: P-NpGal / o-nitrophenyl beta-D-galactopyranoside


organism: Trichoderma reesei

assay_conditions_summary: pH 5; buffer 50 mM acetate

column_label: Table 2, row o-Nitrophenyl-beta-D-galactopyranoside, columns Km (mM), Vmax (nkat mg^-1), and kcat (s^-1), cells 0.36 +/- 0.01, 144.61 +/- 0.15, and 17.31 +/- 0.02.

normalized_value_unit_evidence: Km 0.36 mM; kcat 17.31 s^-1; Vmax 144.61 nkat mg^-1 = 0.00014461 mol s^-1 g^-1. Current export Vmax is 0.00011461 mol s^-1 g^-1, so Vmax needs correction.

raw_value_unit_evidence: Table 2 row o-Nitrophenyl-beta-D-galactopyranoside: Km = 0.36 +/- 0.01 mM; Vmax = 144.61 +/- 0.15 nkat mg^-1; kcat = 17.31 +/- 0.02 s^-1.

row_label: o-Nitrophenyl-beta-D-galactopyranoside

table_label: Table 2: Kinetic parameters of H. jecorina beta-galactosidase with various beta-galactosides

unit: lgwedgeoneswedgeone


organism: uncultured microorganism


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl beta-D-fucopyranoside

substrate: 4-nitrophenyl beta-D-fucopyranoside


organism: Saccharolobus solfataricus


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F441Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F359Q to reconstruct the assayed variant sequence.


proof_lines:
Raw SKiD Env: Temp=30°C, pH=6.5
Raw SKiD Env: Temp=80°C, pH=7.5


organism: Streptococcus thermophilus


substrate_name: Methyl beta-D-galactoside

column_label: Table 3 row Methyl beta-D-galactopyranoside, columns Km=23 mM, kcat=242 min^-1, kcat/Km=10.5 min^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=23 normalized_unit=mM; kcat normalized_value=4.033333333333333 normalized_unit=s^-1; kcat/Km normalized_value=0.175 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=23 raw_unit=mM; kcat raw_value=242 raw_unit=min^-1; kcat/Km raw_value=10.5 raw_unit=min^-1*mM^-1

row_label: Methyl beta-D-galactopyranoside

substrate: Methyl beta-D-galactoside


substrate_name: o-Nitrophenyl-beta-D-galactoside

substrate: o-Nitrophenyl-beta-D-galactoside


substrate_name: alpha-Lactose

column_label: Table 3 row alpha-Lactose, columns Km=13 mM, kcat=114 min^-1, kcat/Km=8.7 min^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=13 normalized_unit=mM; kcat normalized_value=1.9 normalized_unit=s^-1; kcat/Km normalized_value=0.145 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=13 raw_unit=mM; kcat raw_value=114 raw_unit=min^-1; kcat/Km raw_value=8.7 raw_unit=min^-1*mM^-1

row_label: alpha-Lactose

substrate: alpha-Lactose


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant I-cell disease


organism: Kluyveromyces lactis

sequence_source: UniProtKB reviewed (Swiss-Prot) canonical sequence


organism: Kluyveromyces marxianus


organism: Lactobacillus casei


organism: Lactobacillus delbrueckii

substrate_name: lactose


organism: Oryza sativa

proof_lines: pH 3.5, 60°C, recombinant isozyme OsGal1


substrate_name: o-nitrophenyl-beta-D-galactoside

proof_lines:
isoenzyme betaG41
isoenzyme betaG630
isoenzyme betaG550

substrate: o-nitrophenyl-beta-D-galactoside


organism: Pantoea agglomerans

column_label: PMID 17336932 characterization paragraph, Bga/oNPGal segment, Km = 0.06 mM and Vmax = 0.43 mM/min.

raw_value_unit_evidence: The Km and Vmax values for oNPGal were calculated as 0.06 mM and 0.43 mM/min, respectively.

row_label: Bga beta-galactosidase with oNPGal substrate

table_label: Characterization of the enzyme paragraph


organism: Pediococcus pentosaceus

substrate_name: H2O; Lactose


organism: Putranjiva roxburghii


substrate_name: cellobiose

substrate: cellobiose


organism: Raphanus sativus

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

assay_conditions_summary: pH 4; buffer 50 mM acetate

column_label: PMID 16666809 Kinetics section below Table III: PNP-beta-D-Gal row/prose gives Km = 0.46 and Vmax = 5.36 under the units Km (mM) and Vmax (umol/min/mg).

raw_value_unit_evidence: Kinetics prose reports: PNP-beta-D-Gal, Km = 0.46, Vmax = 5.36. The sentence header defines the units as Km (mM) and Vmax (umol/min/mg).

table_label: Kinetics prose below Table III

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


organism: Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)

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

assay_conditions_summary: pH 6


organism: Enterobacter agglomerans

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)


organism: Geobacillus kaustophilus

substrate_name: ONPG (at 55 degrees Celsius and pH 7.0)

substrate: ONPG (at 55 degrees Celsius and pH 7.0)


organism: Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)

substrate_name: ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)


organism: Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 37 degrees Celsius and pH 6.0)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA)

substrate_name: ONPG (at 60 degrees Celsius and pH 6.0)

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

substrate: ONPG (at 60 degrees Celsius and pH 6.0)


organism: Arthrobacter sp

substrate_name: ONPG (at 10 degrees Celsius)

substrate: ONPG (at 10 degrees Celsius)


substrate_name: ONPG

substrate: ONPG


organism: Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)

substrate_name: ONPG (at 30 degrees Celsius and pH 6.5)

substrate: ONPG (at 30 degrees Celsius and pH 6.5)


organism: Bacillus subtilis (strain 168)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius)


organism: Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)

substrate_name: Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0)


substrate: lactose


organism: Carnobacterium maltaromaticum

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 30 degrees Celsius)


organism: Escherichia coli

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201F-

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg ab

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg_b

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg_a


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

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


substrate_name: o-Nitrophenyl-beta-D-galactoside

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E461H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: o-Nitrophenyl-beta-D-galactoside; H2O

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461K

substrate: o-Nitrophenyl-beta-D-galactoside; H2O


substrate_name: p-Nitrophenyl-beta-D-galactoside

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature E461D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 30 mM

column_label: Table I: Kinetic constants and rate constants obtained for the beta-galactosidases with ONPG and PNPG as substrates (Journal of Biological Chemistry 1990, volume 265, number 10, pages 5512-5518); the PNPG substrate block; column head 'ASD' is the Asp substitution, the E461D-beta-galactosidase enzyme; the k_cat stub of that block, rendered 'k,, (s-l)', holds 0.007 in that column; the 'Km (mM)' stub holds 0.011 in that column; the block carries no kcat/Km stub

normalized_value_unit_evidence: kcat: printed Table I cell 0.007 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 0.007 s^(-1). Km: printed Table I cell 0.011 mM; the cell is already in mM, so no unit conversion applies; the exported value is 0.011 mM. kcat/Km: this paper prints no efficiency cell anywhere, so the catalog value is typed as the same-measurement quotient of the two printed cells of this one column, 0.007 / 0.011 = 0.6363636363636365 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Table I, PNPG block, column headed ASD (Asp), the E461D-beta-galactosidase enzyme: the k_cat stub prints 0.007 with the block unit s^-1, and the Km stub prints 0.011 with the block unit mM. Table I prints no catalytic-efficiency column.

row_label: Table I, PNPG substrate block, the k_cat and Km stubs read across to the column headed ASD, which is the Asp substitution, the E461D-beta-galactosidase enzyme

substrate: p-Nitrophenyl-beta-D-galactoside


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature E461K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I: Kinetic constants and rate constants obtained for the beta-galactosidases with ONPG and PNPG as substrates (Journal of Biological Chemistry 1990, volume 265, number 10, pages 5512-5518); the PNPG substrate block; column head 'LYS' is the Lys substitution, the E461K-beta-galactosidase enzyme; the k_cat stub of that block, rendered 'k,, (s-l)', holds 0.24 in that column; the 'Km (mM)' stub holds 0.008 in that column; the block carries no kcat/Km stub

normalized_value_unit_evidence: kcat: printed Table I cell 0.24 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 0.24 s^(-1). Km: printed Table I cell 0.008 mM; the cell is already in mM, so no unit conversion applies; the exported value is 0.008 mM. kcat/Km: this paper prints no efficiency cell anywhere, so the catalog value is typed as the same-measurement quotient of the two printed cells of this one column, 0.24 / 0.008 = 30.0 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Table I, PNPG block, column headed LYS (Lys), the E461K-beta-galactosidase enzyme: the k_cat stub prints 0.24 with the block unit s^-1, and the Km stub prints 0.008 with the block unit mM. Table I prints no catalytic-efficiency column.

row_label: Table I, PNPG substrate block, the k_cat and Km stubs read across to the column headed LYS, which is the Lys substitution, the E461K-beta-galactosidase enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E461G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl-beta-D-fucopyranoside

substrate: p-Nitrophenyl-beta-D-fucopyranoside


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357N


organism: Planococcus sp. (strain L4)

substrate_name: ONPG (at 5 degrees Celsius and at pH 6.8)


organism: Planococcus sp. (strain 'SOS Orange')

substrate_name: ONPG (at 1.9 degrees Celsius and at pH 6.5)


organism: Pseudoalteromonas haloplanktis

substrate_name: lactose (at pH 7.5 and at 25 degrees Celsius)


organism: Thermus sp

substrate_name: pNPGal (at 70 degrees Celsius and pH 7.0)


substrate_name: ONPG (at 70 degrees Celsius and pH 7.0)

column_label: PMC HTML reports Km 1.6 mM with ONPG; assay section defines ONPG assays at 70 C in Z buffer pH 7.0

raw_value_unit_evidence: Km raw_value=1.6 raw_unit=mM

row_label: ChBD-BgaA chimeric beta-galactosidase with ONPG

table_label: PMC HTML abstract and Enzymatic assays section

substrate: ONPG (at 70 degrees Celsius and pH 7.0)


organism: Thermus thermophilus

substrate_name: lactose (at pH 6.5 and at 70 degrees Celsius)


enzyme_display_name: glucose-1-phosphate adenylyltransferase

organism: Arabidopsis thaliana

substrate_name: Diphosphate; ADP alpha-D-glucoside

enzyme: glucose-1-phosphate adenylyltransferase

substrate: Diphosphate; ADP alpha-D-glucoside


substrate_name: D-Glucose 1-phosphate; ATP

substrate: D-Glucose 1-phosphate; ATP


substrate_name: ATP; D-Glucose 1-phosphate

substrate: ATP; D-Glucose 1-phosphate


substrate_name: ATP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=37°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7

substrate: ATP


organism: Hordeum vulgare

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

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


organism: Triticum aestivum

substrate_name: ADP alpha-D-glucoside; Diphosphate

substrate: ADP alpha-D-glucoside; Diphosphate


organism: Zea mays

proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant MPss (Q947C0 (maize) 1-199, P23509 (potato) 200-475)

proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant MPss (Q947C0 (maize): 1-199, P23509 (potato): 200-475)

proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant P2M2Pss (Q947C0 (maize): 72-199, P23509 (potato): rest)


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


substrate_name: alpha-D-Glucose 1-phosphate

substrate: alpha-D-Glucose 1-phosphate


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

proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/C114A

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


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/H149S


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/C424V


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/P372A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/V502T


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/D368S


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/E438Q


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/Q213H


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/M172T


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/A508S


organism: Solanum lycopersicum

assay_conditions_summary: cofactor ADP


organism: Solanum tuberosum


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R116A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R381A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R146A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R107A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R340A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R77K


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant R104A


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/C382F


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/T361C


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/V227R


proof_lines: SABIO-RK modifier species: glucose-1-phosphate adenylyltransferase(Enzyme) mutant BT2/S163F


organism: Pseudomonas aeruginosa

substrate_name: amoxicillin (at pH 7.0 and 37 degrees Celsius)


organism: Pseudomonas fluorescens

substrate_name: nitrocefin

assay_conditions_summary: buffer qualifiers in the batch payload

substrate: nitrocefin


organism: Escherichia coli (strain K12)

proof_lines: kcat is 111 sec(-1) for adenylyltransferase activity. kcat is 81 sec(-1) for pyrophosphorylase activity.


substrate_name: para-nitrophenyl-beta-D-galactoside

proof_lines: Measured at pH 4.5 and 37 degrees Celsius for all experiments.

substrate: para-nitrophenyl-beta-D-galactoside


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: ATP; alpha-D-glucose 1-phosphate

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

substrate: ATP; alpha-D-glucose 1-phosphate


organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)

substrate_name: lactose

substrate: lactose


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

substrate_name: Gal-beta-PNP

substrate: Gal-beta-PNP


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

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

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


substrate_name: p-nitrophenyl beta-D-galactoside

proof_lines: The values for the enzymatic assays using manganese as cofactor are very close.

substrate: p-nitrophenyl beta-D-galactoside


substrate_name: ADP

substrate: ADP


organism: Brassica napus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 8; 297.15 K; cofactor ATP

substrate: Phosphoenolpyruvate; ADP


organism: Canis familiaris

substrate_name: ADP; Phosphoenolpyruvate

assay_conditions_summary: cofactor ATP

substrate: ADP; Phosphoenolpyruvate


organism: Trichoderma reesei

proof_lines:
pH 7.5, 30°C, isozyme BGT I
pH 7.5, 35°C, isozyme BGT I
pH 7.5, 35°C, isozyme BGT II


organism: Homo sapiens

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Thermofilum pendens

assay_conditions_summary: pH 6; 318.15 K; buffer His6 tag' and related; cofactor ADP

proof_lines: pH 6.0, 45°C, recombinant enzyme with His6 tag


organism: Trachemys scripta elegans

proof_lines:
muscle enzyme, pH 7.2, 22°C
muscle enzyme, pH 6.6, 22°C
liver enzyme, pH 6.6, 22°C


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant L76R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R22G


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R19Q


organism: Agrobacterium tumefaciens

substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, wild-type enzyme in presence of 0.3 mM fructose-1,6-bisphosphate


organism: Anabaena sp.

assay_conditions_summary: pH 7.5; 278.15 K; cofactor ATP

proof_lines:
pH 7.5, 5°C, kinetic study
pH 7.0, 37°C, kinetic study
pH 7.5, 30°C, kinetic study


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; cofactor ATP


assay_conditions_summary: pH 7.9; cofactor ATP

proof_lines: pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate

proof_lines: pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate

proof_lines: pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate


organism: Escherichia coli

substrate_name: Unknown

proof_lines: pH 7.0, 37°C, double mutant enzyme P295D/G336D

substrate: Unknown


proof_lines: pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme

proof_lines: pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme

proof_lines: pH 7.0, 37°C, strain AC70R1, kinetic study

substrate: ATP


proof_lines: mutant Q106A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: mutant Q106A, S0.5 value, Hill coefficient 1.6, pH 8.0, 37°C

proof_lines: mutant Q106A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C


proof_lines: pH 7.0, 37°C, mutant enzyme P295Q, in the presence of a saturating concentration of fructose 1,6-bisphosphate


proof_lines: pH 7.0, 37°C, mutant enzyme P295G, in the presence of a saturating concentration of fructose 1,6-bisphosphate,


organism: Aeromonas caviae

proof_lines: in presence of 0.5 mM fructose 6-phosphate


organism: Aeromonas hydrophila

proof_lines: pH 8.0, 37°C, in presence of fructose 1,6-bisphosphate

proof_lines: pH 8.0, 37°C, in presence of fructose 6-phosphate


proof_lines: pH 8.0, 37°C, the chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme is slightly activated by AMP in the range of 0.1-2 mM


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: pH 7.0, 37°C, mutant enzyme P295N, in the presence of a saturating concentration of fructose 1,6-bisphosphate


proof_lines: mutant P103A, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: mutant P103A, S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C

proof_lines: mutant P103A, S0.5 value, Hill coefficient 1.5, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C


proof_lines: mutant R107A, S0.5 value, Hill coefficient 1.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: mutant R107A, S0.5 value, Hill coefficient 0.9, pH 8.0, 37°C

proof_lines: mutant R107A, S0.5 value, Hill coefficient 2.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C


proof_lines: mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: mutant R115A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C

proof_lines: mutant R115A, S0.5 value, Hill coefficient 2.1, pH 8.0, 37°C


proof_lines: mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C


proof_lines: pH 7.0, 37°C, mutant enzyme P295D, in the presence of a saturating concentration of fructose 1,6-bisphosphate


proof_lines: mutant Y114A, S0.5 value, Hill coefficient 0.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: mutant Y114A, S0.5 value, Hill coefficient 0.3, pH 8.0, 37°C

proof_lines: mutant Y114A, S0.5 value, Hill coefficient 1.9, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C


proof_lines: mutant W113A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C


proof_lines: pH 7.0, 37°C, mutant enzyme G336D, in the presence of a saturating concentration of fructose 1,6-bisphosphate


organism: Auxenochlorella pyrenoidosa

proof_lines: pH 8.5, in absence of 3-phosphoglycerate

proof_lines: pH 8.5, in presence of 2 mM 3-phosphoglycerate


organism: Cereibacter sphaeroides

proof_lines: pH 8, 37°C, in absence of fructose 6-phosphate

proof_lines: pH 8, 37°C, in presence of fructose 6-phosphate

proof_lines: pH 8, 37°C, enzyme modified for 30 min with 5 mM 2,3-butanedione


organism: Chlamydomonas reinhardtii

proof_lines: pH 8.0, 37°C, in absence of 3-phosphoglycerate

proof_lines: pH 8.0, 37°C, in presence of 0.25 mM 3-phosphoglycerate


organism: Citrobacter freundii

assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP

proof_lines: pH 8.4, 37°C, influence of activators on Km


proof_lines: pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes

proof_lines: wild-type, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C


organism: Hafnia alvei

proof_lines: pH 8.0, 37°C, in absence of phosphoenolpyruvate

proof_lines: pH 8.0, 37°C, in presence of phosphoenolpyruvate