substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


enzyme_display_name: mannitol 2-dehydrogenase (NADP(+))

organism: Alternaria alternata

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: plusminus 0.0035 mM, pH 7.0, room temperature

enzyme: mannitol 2-dehydrogenase (NADP(+))

status: unverified

source: brenda


substrate_name: D-fructose

assay_conditions_summary: pH 7

proof_lines: plusminus 80 mM, pH 7.0, room temperature

substrate: D-fructose


enzyme_display_name: sorbitol-6-phosphate 2-dehydrogenase

organism: Escherichia coli

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

enzyme: sorbitol-6-phosphate 2-dehydrogenase

substrate: NAD+


substrate_name: D-sorbitol 6-phosphate

substrate: D-sorbitol 6-phosphate


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Bos taurus

substrate_name: prostaglandin E1

substrate: prostaglandin E1


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Canis lupus familiaris

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

proof_lines:
enzyme from kidney
kidney enzyme, pH 7.4, 37°C
enzyme from heart


organism: Homo sapiens

mutation_type: substitution

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


proof_lines:
37°C, pH 7.5
recombinant enzyme expressed in E. coli
at pH 9.0, + prostaglandin E2


proof_lines:
37°C, pH 7.5
substrate prostaglandin E1


substrate_name: prostaglandin A1

substrate: prostaglandin A1


proof_lines:
at pH 7.0
at pH 9.0
recombinant enzyme expressed in E. coli


substrate_name: Prostaglandin A2

substrate: Prostaglandin A2


substrate_name: prostaglandin E2

proof_lines: pH 8.0, 25°C, 20 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone

proof_lines: pH 8.0, 25°C, 10 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine

proof_lines: pH 8.0, 25°C, 10 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone

substrate: prostaglandin E2


substrate_name: prostaglandin F2alpha

substrate: prostaglandin F2alpha


smiles: CCCCCC(C=CC=CCC=CCCCC(=O)O)O


assay_conditions_summary: pH 7; cofactor NADH

proof_lines:
at pH 7.0, + 15-keto-PGE1
at pH 7.0, + 15-ketoprostaglandin E2
at pH 9.0, + 15-ketoprostaglandin E2


substrate_name: 15-ketoprostaglandin E2

assay_conditions_summary: pH 9

proof_lines:
at pH 9.0
at pH 7.0

substrate: 15-ketoprostaglandin E2


substrate_name: 15-ketoprostaglandin E1

substrate: 15-ketoprostaglandin E1


substrate_name: 6-oxo-prostaglandin F1alpha

substrate: 6-oxo-prostaglandin F1alpha


organism: Sus scrofa


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

proof_lines: prostaglandin E2 as the variable substrate


substrate_name: allopregnanolone

substrate: allopregnanolone


substrate_name: androstenediol

substrate: androstenediol


substrate_name: dehydroepiandrosterone

proof_lines: microsomes mitochondria

substrate: dehydroepiandrosterone


substrate_name: pregnenolone

proof_lines: mitochondria microsomes

substrate: pregnenolone


substrate_name: NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: progesterone

substrate: progesterone


substrate_name: testosterone

substrate: testosterone


substrate_name: 13,14-dihydro-15-keto-prostaglandin F2

substrate: 13,14-dihydro-15-keto-prostaglandin F2


substrate_name: androstenedione

substrate: androstenedione


substrate_name: D-glucose

substrate: D-glucose


substrate_name: prostaglandin E1

substrate: prostaglandin E1


substrate_name: D-glucuronic acid

substrate: D-glucuronic acid


substrate_name: D-xylose

substrate: D-xylose


substrate_name: Camphorquinone

substrate: Camphorquinone


substrate_name: caprinaldehyde

smiles: CCCCCCCCCC=O

substrate: caprinaldehyde


substrate_name: menadione

substrate: menadione


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


enzyme_display_name: 11beta-hydroxysteroid dehydrogenase

organism: Rattus norvegicus

substrate_name: corticosterone

proof_lines: 37°C, pH 7.4, in HEK-293 lysates expressing 11beta-HSD1

enzyme: 11beta-hydroxysteroid dehydrogenase

substrate: corticosterone


proof_lines: i.e. cortisol,temperature not specified in the publication, pH 9


proof_lines: i.e. cortisone, temperature not specified in the publication, pH 9


substrate_name: NADPH

assay_conditions_summary: pH 9; cofactor NADPH

proof_lines: temperature not specified in the publication, pH 9

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: pH 9; cofactor NADP+

substrate: NADP+


organism: Rattus sp.

proof_lines: reduction of corticosterone, ordered sequential mechanism


substrate_name: NAD+

substrate: NAD+


proof_lines:
at pH 7.0
at pH 8.5
isoform 11beta-HSD1


substrate_name: cortisol

assay_conditions_summary: 310.15 K; cofactor NADP+

proof_lines: enzyme from caput epididymidis, cosubstrate NADP+, 37°C, pH not specified in the publication

proof_lines: enzyme from testis, cosubstrate NADP+, 37°C, pH not specified in the publication

proof_lines: enzyme from bulbourethral gland, cosubstrate NADP+, 37°C, pH not specified in the publication

substrate: cortisol


enzyme_display_name: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

organism: Drosophila melanogaster

substrate_name: sepiapterin

substrate: sepiapterin


assay_conditions_summary: pH 8.1; 303.15 K; cofactor NAD+


substrate_name: (S)-ureidoglycolate

substrate: (S)-ureidoglycolate


enzyme_display_name: 7alpha-hydroxysteroid dehydrogenase

substrate_name: cholic acid

enzyme: 7alpha-hydroxysteroid dehydrogenase

substrate: cholic acid


substrate_name: glycocholic acid

substrate: glycocholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


substrate_name: taurochenodeoxycholic acid

substrate: taurochenodeoxycholic acid


substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


substrate_name: glycochenodeoxycholic acid

substrate: glycochenodeoxycholic acid


enzyme_display_name: 2-dehydropantoate 2-reductase

substrate_name: thio-NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
pH 7.5, 25°C, recombinant enzyme
pH 7.6

enzyme: 2-dehydropantoate 2-reductase

substrate: thio-NADPH


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


assay_conditions_summary: pH 7.5; 300.15 K; cofactor NADPH


substrate_name: ketopantoate

substrate: ketopantoate


proof_lines:
+/-0.009, mutant K176C, alkylated
+/-0.01, mutant K176C


substrate_name: Pantoate

substrate: Pantoate


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: ketopantoic acid

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

substrate: ketopantoic acid


organism: Staphylococcus aureus


organism: Stenotrophomonas maltophilia


substrate_name: D-pantoic acid

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

assay_conditions_summary: pH 8

substrate: D-pantoic acid


enzyme_display_name: D-xylose 1-dehydrogenase

organism: Caulobacter vibrioides

enzyme: D-xylose 1-dehydrogenase


substrate_name: D-xylose

proof_lines:
at pH 7.0 and 25°C
25°C, pH 6.8
25°C, pH 9.0

substrate: D-xylose


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Pseudomonas sp.

proof_lines:
strain 89B
strain 90A


proof_lines:
strain 90A
strain 89B


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)

substrate_name: D-arabinose

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

substrate: D-arabinose


substrate_name: D-galactose

enzyme: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)

substrate: D-galactose


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


substrate_name: D-ribose

assay_conditions_summary: buffer context

substrate: D-ribose


substrate_name: NADP+

substrate: NADP+


organism: Trichoderma reesei

substrate_name: D-glucose

substrate: D-glucose


assay_conditions_summary: pH 8.1; 303.15 K; cofactor NADP+


enzyme_display_name: carbonyl reductase (NADPH)

substrate_name: daunorubicin

enzyme: carbonyl reductase (NADPH)

substrate: daunorubicin


substrate_name: menadione

substrate: menadione


substrate_name: all-trans-retinol

substrate: all-trans-retinol


assay_conditions_summary: pH 6


substrate_name: isatin

substrate: isatin


substrate_name: heptanophenone

substrate: heptanophenone


substrate_name: valerophenone

substrate: valerophenone


substrate_name: acenaphthenequinone

substrate: acenaphthenequinone


substrate_name: n-butyrophenone

substrate: n-butyrophenone


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


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


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


substrate_name: hexanophenone

substrate: hexanophenone


substrate_name: benzoylformic acid ethyl ester

substrate: benzoylformic acid ethyl ester


organism: Cavia porcellus

substrate_name: pyridine 4-aldehyde

assay_conditions_summary: cofactor NADPH

proof_lines:
cofactor NADPH
cofactor NADH

substrate: pyridine 4-aldehyde


substrate_name: pyridine 3-aldehyde

proof_lines:
cofactor NADPH
cosubstrate NADH

substrate: pyridine 3-aldehyde


substrate_name: Benzalacetone

substrate: Benzalacetone


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: acetone

smiles: CC(=O)C

substrate: acetone


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


organism: Cricetulus griseus

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH

proof_lines: at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C


substrate_name: NADPH

substrate: NADPH


substrate_name: NADH

substrate: NADH


substrate_name: menadione

substrate: menadione


organism: Gallus gallus


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


substrate_name: estrone

substrate: estrone


substrate_name: testosterone

substrate: testosterone


substrate_name: prostaglandin E2

substrate: prostaglandin E2


substrate_name: isatin

substrate: isatin


substrate_name: p-toluquinone

substrate: p-toluquinone


proof_lines: wild-type CBR3 and mutant V244M. Residues 262-277, 236-244/262-277 or 230 of CBR3 exchanged to the corresponding amino acids of CBR1


proof_lines: after treatment with S-nitrosoglutathione, pH 7.4, 25°C

proof_lines: enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C


proof_lines: residues 142-143, 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1


substrate_name: oracin

substrate: oracin


substrate_name: daunorubicin

substrate: daunorubicin


proof_lines:
wild-type, pH 7.4, 25°C
wild-type, pH 7.4, 37°C


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


proof_lines: wild-type, pH 7.4, temperature not specified in the publication


substrate_name: doxorubicin

proof_lines: single nucleotide polymorphism V88I mutation

substrate: doxorubicin


proof_lines: single nucleotide polymorphism P131S mutation


substrate_name: benzoylpyridine

substrate: benzoylpyridine


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


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


substrate_name: S-nitrosoglutathione

proof_lines: mutant C227S, pH 7.4, temperature not specified in the publication

substrate: S-nitrosoglutathione


proof_lines: mutant D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P, pH 7.4, temperature not specified in the publication


proof_lines: mutant P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244PpH 7.4, temperature not specified in the publication


proof_lines: mutant Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S, pH 7.4, temperature not specified in the publication


substrate_name: Prostaglandin B2

substrate: Prostaglandin B2


substrate_name: 4-formylbenzoic acid

substrate: 4-formylbenzoic acid


proof_lines:
wild-type
wild-type, pH 7.4, 25°C
wild-type, pH 7.4, 37°C


proof_lines:
pH 6.5, 25°C
Km depending on enzyme form


substrate_name: prostaglandin E1

substrate: prostaglandin E1


proof_lines:
in stomach
in kidney
in colon


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


organism: Oryctolagus cuniculus


substrate_name: loxoprofen

substrate: loxoprofen


substrate_name: acetohexamide

substrate: acetohexamide


substrate_name: befunolol

substrate: befunolol


substrate_name: NADPH

substrate: NADPH


substrate_name: menadione

substrate: menadione


substrate_name: hexaphenone

proof_lines:
pH 6.0, 25°C, recombinant enzyme
pH 6.0, recombinant enzyme
pH 6.0, 37°C

substrate: hexaphenone


substrate_name: heptanophenone

proof_lines:
pH 6.0, recombinant enzyme
pH 6.0, 37°C

substrate: heptanophenone


substrate_name: isatin

substrate: isatin


substrate_name: nonanophenone

substrate: nonanophenone


substrate_name: benzil

substrate: benzil


proof_lines:
pH 6.0, 25°C, recombinant enzyme
pH 6.0, recombinant enzyme


substrate_name: diacetyl

substrate: diacetyl


substrate_name: pyridin-4-yl hexanoate

substrate: pyridin-4-yl hexanoate


proof_lines:
pH 7.4, 37°C
pH 6.0, 25°C, recombinant enzyme
pH 6.0, recombinant enzyme


substrate_name: valerophenone

proof_lines:
pH 6.0, 37°C
pH 6.0, 25°C, recombinant enzyme
pH 6.0, recombinant enzyme

substrate: valerophenone


substrate_name: butyrophenone

substrate: butyrophenone


substrate_name: propiophenone

substrate: propiophenone


substrate_name: Adrenochrome

substrate: Adrenochrome


substrate_name: prostaglandin E2

substrate: prostaglandin E2


enzyme_display_name: prostaglandin-E2 9-reductase

organism: Bos taurus

enzyme: prostaglandin-E2 9-reductase


proof_lines: competitive inhibitor for the reduction of 20alpha-hydroxy-pregn-4-en-3-one to progesterone


substrate_name: DL-glyceraldehyde

substrate: DL-glyceraldehyde


substrate_name: methylglyoxal

substrate: methylglyoxal


organism: Escherichia coli


enzyme_display_name: coniferyl-alcohol dehydrogenase

organism: Streptomyces sp.

substrate_name: coniferyl alcohol

enzyme: coniferyl-alcohol dehydrogenase

substrate: coniferyl alcohol


enzyme_display_name: cinnamyl-alcohol dehydrogenase

organism: Arabidopsis thaliana

proof_lines: mutant T49A, 30°C, pH not specified in the publication

enzyme: cinnamyl-alcohol dehydrogenase


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


proof_lines: mutant H52A, 30°C, pH not specified in the publication


proof_lines: mutant D57A, 30°C, pH not specified in the publication


organism: Medicago truncatula

substrate_name: sinapyl aldehyde

proof_lines: Mt-CAD2, pH and temperature not specified in the publication

substrate: sinapyl aldehyde


proof_lines: Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


substrate_name: p-coumaryl aldehyde

substrate: p-coumaryl aldehyde


proof_lines: wild-type Mt-CAD2, pH and temperature not specified in the publication


organism: Oryza sativa

proof_lines: pH 8.8, 30°C, recombinant enzyme encoded by GH2


organism: Oryza sativa Japonica Group


substrate_name: 4-coumaryl aldehyde

substrate: 4-coumaryl aldehyde


substrate_name: cinnamyl aldehyde

substrate: cinnamyl aldehyde


organism: Panicum virgatum

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


substrate_name: coumaryl alcohol

substrate: coumaryl alcohol


substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


organism: Pinus taeda

substrate_name: coniferaldehyde

substrate: coniferaldehyde


substrate_name: NADPH

proof_lines:
with coniferaldehyde
with cinnamaldehyde

substrate: NADPH


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: sinapaldehyde

substrate: sinapaldehyde


organism: Sorghum bicolor

proof_lines: isoform CAD4 mutant Y288P, at pH 6.5 and 30°C


proof_lines: wild type isoform CAD4, at pH 6.5 and 30°C

proof_lines: wild type isoform CAD2, at pH 6.5 and 30°C


proof_lines: isoform CAD4 mutant W58L, at pH 6.5 and 30°C


proof_lines: isoform CAD4 mutant Y95V, at pH 6.5 and 30°C


proof_lines: isoform CAD4 mutant G301F, at pH 6.5 and 30°C


proof_lines: isoform CAD4 mutant L119W/G301F, at pH 6.5 and 30°C


proof_lines: pH 8.8, temperature not specified in the publication


organism: Triticum aestivum

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


substrate_name: 5-hydroxyconiferyl aldehyde

substrate: 5-hydroxyconiferyl aldehyde


substrate_name: caffeoyl aldehyde

substrate: caffeoyl aldehyde


substrate_name: p-coumaryl alcohol

proof_lines:
isoform CAD-C
purified isoform CAD-C
isoform CAD-B

substrate: p-coumaryl alcohol


proof_lines:
purified isoform CAD-C
isoform CAD-B
isoform CAD-A


proof_lines:
purified isoform CAD-C
isoform CAD-C
isoform CAD-B


organism: Sus scrofa

substrate_name: NADP+

substrate: NADP+


substrate_name: Prostaglandin D2

substrate: Prostaglandin D2


substrate_name: prostaglandin D1

substrate: prostaglandin D1


substrate_name: prostaglandin E2

substrate: prostaglandin E2


substrate_name: prostaglandin F2alpha

substrate: prostaglandin F2alpha


substrate_name: prostaglandin I2

substrate: prostaglandin I2


enzyme_display_name: 1,3-propanediol dehydrogenase

organism: Citrobacter freundii

substrate_name: NADH

assay_conditions_summary: cofactor NADH

enzyme: 1,3-propanediol dehydrogenase

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


smiles: C(CO)CO


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


smiles: C(CO)C=O

proof_lines: pH and temperature not specified in the publication


organism: Clostridium butyricum

assay_conditions_summary: pH 9; 310.15 K; cofactor NADH

proof_lines: with propionaldehyde as cosubstrate, at pH 9.0 and 37°C


assay_conditions_summary: pH 11; 303.15 K; cofactor NAD+

proof_lines: with propane-1,3-diol as cosubstrate, at pH 11.0 and 30°C


organism: Klebsiella pneumoniae

substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


assay_conditions_summary: pH 7; 310.15 K; cofactor NADH


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH


substrate_name: NADPH

substrate: NADPH


assay_conditions_summary: pH 9; 328.15 K; cofactor NAD+

proof_lines:
pH 9.0, 55°C
pH 9.5, 30°C, recombinant enzyme


enzyme_display_name: uronate dehydrogenase

organism: Agrobacterium tumefaciens

substrate_name: beta-D-glucuronate

enzyme: uronate dehydrogenase

substrate: beta-D-glucuronate


proof_lines: mutant enzyme H101N/H236K, at pH 8.0 and 25°C


proof_lines: mutant enzyme A41P/H101Y/H236K, at pH 8.0 and 25°C


proof_lines: mutant enzyme A41P/H101N/H236K, at pH 8.0 and 25°C


proof_lines: mutant enzyme H101Y/H236K, at pH 8.0 and 25°C


proof_lines: mutant enzyme A41P/H101Y/H236R, at pH 8.0 and 25°C


proof_lines: mutant enzyme A41P/H101N/H236R, at pH 8.0 and 25°C


proof_lines: mutant enzyme A41P/H236K, at pH 8.0 and 25°C


substrate_name: D-glucuronic acid

substrate: D-glucuronic acid


proof_lines: mutant enzyme A39P/H99Y, at pH 8.0 and 30°C


proof_lines: mutant enzyme A39P/H234K, at pH 8.0 and 30°C


proof_lines: mutant enzyme H99Y/H234K, at pH 8.0 and 30°C


proof_lines: mutant enzyme A39P/H99Y/H234K, at pH 8.0 and 30°C


substrate_name: beta-D-galacturonate

assay_conditions_summary: buffer recombinant His-tagged enzyme

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

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

substrate: beta-D-galacturonate


assay_conditions_summary: buffer potassium phosphate; cofactor NAD+


substrate_name: D-galacturonate

substrate: D-galacturonate


organism: Pseudomonas fluorescens


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Pseudomonas syringae


enzyme_display_name: IMP dehydrogenase

organism: Bacillus amyloliquefaciens

assay_conditions_summary: pH 8; 313.15 K; cofactor NAD+

proof_lines: pH 8.0, 40°C, recombinant wild-type enzyme and mutant K481E

proof_lines: pH 8.0, 40°C, recombinant wild-type enzyme and mutant P166S

proof_lines: pH 8.0, 40°C, recombinant wild-type enzyme and mutant IMPDHDELTACBS

enzyme: IMP dehydrogenase


substrate_name: IMP

proof_lines: pH 8.0, 40°C, recombinant wild-type enzyme and mutant P166S and K481E

proof_lines: pH 8.0, 40°C, recombinant wild-type enzyme, and recombinant mutant enzymes, P166S, K481E, and IMPDHDELTACBS

substrate: IMP


proof_lines: pH 8.0, 40°C, recombinant mutant enzyme IMPDHDELTACBS

proof_lines: pH 8.0, 40°C, recombinant mutant IMPDHDELTACBS


organism: Bacillus anthracis

mutation_type: deletion

proof_lines: pH 8.0, 25°C, recombinant long enzyme CBS-deletion mutant BaIMPDHDELTAL


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme


proof_lines: pH 8.0, 25°C, recombinant short enzyme CBS-deletion mutant BaIMPDHDELTAS


mutation_signature: recombinant long enzyme CBS-deletion mutant BaIMPDHDELTAL


mutation_signature: recombinant short enzyme CBS-deletion mutant BaIMPDHDELTAS


proof_lines: pH 8.0, 30°C, recombinant enzyme, without MgATP2-

proof_lines: pH 8.0, 30°C, recombinant enzyme, with MgATP2-


substrate_name: Unknown

proof_lines: substrate inosine monophosphate, pH 8.0, 22°C

substrate: Unknown


substrate_name: Inosine 5'-diphosphate

substrate: Inosine 5'-diphosphate


organism: Bacillus subtilis


substrate_name: K+

substrate: K+


organism: Campylobacter jejuni


proof_lines: pH 8.0, 25°C, recombinant short enzyme CBS-deletion mutant CjIMPDHDELTAS


mutation_signature: recombinant short enzyme CBS-deletion mutant CjIMPDHDELTAS


organism: Candida albicans


organism: Clostridium perfringens

proof_lines: pH 8.0, 25°C, recombinant short enzyme CBS-deletion mutant ClpIMPDHDELTAL


mutation_signature: recombinant short enzyme CBS-deletion mutant ClpIMPDHDELTAL


organism: Cricetulus griseus


organism: Escherichia coli


proof_lines: chemically synthesized thiazole-4-carboxamide adenine dinucleotide

proof_lines: with thiazole-4-carboxamide adenine dinucleotide synthesized chemically

proof_lines: enzymatically synthesized thiazole-4-carboxamide adenine dinucleotide


substrate_name: inosine 5'-phosphate

substrate: inosine 5'-phosphate


organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme

substrate: NAD+


substrate_name: beta-NAD+

proof_lines: pH 8.0, 37°C, recombinant mutants D226N and V268I

substrate: beta-NAD+


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Leishmania donovani


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


organism: Mus musculus

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


proof_lines:
for the competitive component
for the non-competitive component
pH 8.0, 37°C


organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines:
recombinant enzyme, pH 8.5, 37°C
pH 8.0, 25°C


proof_lines: pH and temperature not specified in the publication


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


assay_conditions_summary: pH 8; 295.15 K; cofactor NAD+


proof_lines: recombinant MtbIMPDH2DELTACBS mutant enzyme, pH 8.0, 22°C


organism: Neisseria meningitidis


organism: Penicillium brevicompactum

proof_lines: wild type enzyme isoform IMPDHA, at pH 8.0 and 25°C


organism: Rattus norvegicus


assay_conditions_summary: cofactor NAD+


proof_lines:
versus inosine 5'-phosphate
versus NAD+


organism: Staphylococcus aureus

proof_lines: pH 8.0, 30°C, recombinant enzyme, without MgATP2-

proof_lines: pH 8.0, 30°C, recombinant enzyme, with MgATP2-


organism: Streptococcus pyogenes


organism: Sus scrofa


organism: Toxoplasma gondii


organism: Trypanosoma brucei


substrate_name: androsterone

substrate: androsterone


substrate_name: testosterone

substrate: testosterone


proof_lines:
wild-type
wild-type, pH 7.0, 25°C


substrate_name: Epitestosterone

substrate: Epitestosterone


assay_conditions_summary: cofactor NADP+


substrate_name: glycolithocholic acid

substrate: glycolithocholic acid


substrate_name: NADP+

substrate: NADP+


substrate_name: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


substrate_name: Naphthalene dihydrodiol

substrate: Naphthalene dihydrodiol


substrate_name: lithocholic acid

substrate: lithocholic acid


organism: Bos taurus

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


enzyme_display_name: dihydroflavanol 4-reductase

organism: Camellia sinensis

substrate_name: (+)-dihydroquercetin

enzyme: dihydroflavanol 4-reductase

substrate: (+)-dihydroquercetin


substrate_name: (+)-dihydromyricetin

substrate: (+)-dihydromyricetin


substrate_name: (+)-dihydrokaempferol

substrate: (+)-dihydrokaempferol


substrate_name: estrone

substrate: estrone


substrate_name: Unknown

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

substrate: Unknown


organism: Phascolarctos cinereus

proof_lines: enzyme avtivity in hepatic microsomes, one individual animal


enzyme_display_name: methanol dehydrogenase

organism: Bacillus methanolicus

assay_conditions_summary: pH 9.5; 323.15 K; cofactor NAD+

proof_lines: recombinant enzyme without added Mg2+, pH 9.5, 50°C

enzyme: methanol dehydrogenase


substrate_name: methanol

smiles: CO

substrate: methanol


proof_lines: recombinant enzyme, pH 9.0, 30°C, in presence of activator Act

proof_lines: recombinant enzyme, pH 7.4, 30°C, in presence of activator Act

proof_lines: recombinant enzyme, pH 9.0, 30°C, in absence of activator Act


substrate_name: ethanol

smiles: CCO

substrate: ethanol


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADP+

proof_lines: recombinant enzyme mutant D38G, pH 7.4, 30°C, in presence of activator Act, with NADP+

proof_lines: recombinant enzyme mutant D38G, pH 7.4, 30°C, in absence of activator Act, with NADP+


proof_lines: recombinant enzyme mutant S98G, pH 7.4, 30°C, in presence of activator Act

proof_lines: recombinant enzyme mutant S98G, pH 7.4, 30°C, in absence of activator Act


enzyme_display_name: codeinone reductase (NADPH)

organism: Papaver somniferum

substrate_name: codeine

assay_conditions_summary: pH 9; 303.15 K; cofactor NADPH

proof_lines:
pH 9.0, 30°C
enzyme from cell culture
isoenzymes from capsule tissue

enzyme: codeinone reductase (NADPH)

substrate: codeine


substrate_name: codeinone

assay_conditions_summary: pH 6.8; 303.15 K; cofactor NADPH

proof_lines:
pH 6.8, 30°C
isoenzymes from capsule tissue
enzyme from cell culture

substrate: codeinone


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


substrate_name: Hydrocodone

proof_lines:
isoenzymes from capsule tissue
morphine, enzyme from cell culture
enzyme from cell culture

substrate: Hydrocodone


substrate_name: Hydromorphone

proof_lines:
isoenzymes from capsule tissue
enzyme from cell culture

substrate: Hydromorphone


substrate_name: morphine

substrate: morphine


substrate_name: Dihydrocodeine

substrate: Dihydrocodeine


enzyme_display_name: glyoxylate reductase

organism: Paracoccus sp. (in: a-proteobacteria)

substrate_name: glyoxylate

proof_lines: pH 7.0, 30°C, recombinant E141N/Q313E mutant formate dehydrogenase

enzyme: glyoxylate reductase

substrate: glyoxylate


organism: Rhizobium etli

substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


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


organism: Escherichia coli


enzyme_display_name: 1,5-anhydro-D-fructose reductase

enzyme: 1,5-anhydro-D-fructose reductase


enzyme_display_name: L-idonate 5-dehydrogenase [NAD(P)(+)]

substrate_name: L-Idonate

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

enzyme: L-idonate 5-dehydrogenase [NAD(P)(+)]

substrate: L-Idonate


organism: Arabidopsis thaliana

substrate_name: NADP+

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: pH 8.0, 37°C, recombinant pseudomature enzyme

substrate: NADP+


substrate_name: 2-C-methyl-D-erythritol 4-phosphate

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

substrate: 2-C-methyl-D-erythritol 4-phosphate


substrate_name: 1-deoxy-D-xylulose 5-phosphate

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

substrate: 1-deoxy-D-xylulose 5-phosphate


substrate_name: NADPH

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


proof_lines: pH 7.6, 37°C, recombinant His-tagged enzyme


substrate_name: 1-fluoro-1-deoxy-D-xylulose 5-phosphate

assay_conditions_summary: pH 7.6; 310.15 K; cofactor NADPH

proof_lines: pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2

proof_lines: pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd4

substrate: 1-fluoro-1-deoxy-D-xylulose 5-phosphate


proof_lines:
pH 7.6, 37°C, recombinant enzyme
with 1 mM MnCl2
with 1 mM CoCl2


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

proof_lines:
pH 7.7, presence of 3 mM MgCl2
pH 7.7, presence of 1 mM MnCl2


organism: Francisella tularensis

assay_conditions_summary: pH 7.8; 295.15 K; cofactor NADPH


organism: Mycobacterium tuberculosis


proof_lines: pH 7.9, 30°C, recombinant His-tagged enzyme


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines: pH 7.5, 25°C, recombinant enzyme, with substrate 1-deoxy-D-xylulose 5-phosphate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
pH 7.5, 25°C, recombinant enzyme
presence of Co2+, pH 7.5, 25°C
presence of Mn2+, pH 7.5, 25°C


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

proof_lines: pH 7.5, 25°C, recombinant enzyme in presence of phosphite dianion

proof_lines: pH 7.5, 25°C, recombinant enzyme in absence of phosphite dianion

proof_lines: pH 7.5, 25°C, recombinant enzyme in absence or presence of phosphite dianion


proof_lines: cosubstrate NADPH, presence of Co2+, pH 7.5, 25°C

proof_lines: cosubstrate NADPH, presence of Mg2+, pH 7.5, 25°C


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines:
presence of Co2+, pH 7.5, 25°C
presence of Mn2+, pH 7.5, 25°C
presence of Mg2+, pH 7.5, 25°C

substrate: NADH


organism: Plasmodium falciparum


enzyme_display_name: 3beta-hydroxysteroid 3-dehydrogenase

organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+

enzyme: 3beta-hydroxysteroid 3-dehydrogenase

substrate: NAD+


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


proof_lines:
3beta-HSD1 wild-type, pH 7.4, 27°C
pH 7.4, 27°C, wild-type enzyme
3beta-HSD2 wild-type, pH 7.4, 27°C


proof_lines: pH 7.0, 37°C, radiometric analysis, formation of 3beta-androstanediol

proof_lines: pH 7.0, 37°C, radiometric analysis, formation of 3alpha-androstanediol

proof_lines: pH 7.0, 37°C, spectrophotometric analysis, formation of 3beta-androstanediol or 3alpha-androstanediol


organism: Rattus norvegicus

proof_lines:
solubilized enzyme
microsomal-bound enzyme


enzyme_display_name: GDP-L-fucose synthase

enzyme: GDP-L-fucose synthase


assay_conditions_summary: cofactor NADH


organism: Escherichia coli K-12


proof_lines: mutant C109S, isotope [5''-2H]-GDP-6-deoxy-4-keto-mannose

proof_lines: mutant C109S, isotope [3''-2H]-GDP-6-deoxy-4-keto-mannose


organism: Helicobacter pylori


organism: Sus scrofa


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

proof_lines: pH 7.0, 30°C, with a cofactor level 20fold higher than the Km value


substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: YqhE YafB

substrate: methylglyoxal


enzyme_display_name: serine 3-dehydrogenase (NADP(+))

organism: Agrobacterium tumefaciens

enzyme: serine 3-dehydrogenase (NADP(+))


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-Glycerate

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

substrate: L-Glycerate


substrate_name: D-glycerate

substrate: D-glycerate


proof_lines:
versus L-serine, pH 9.0, 30°C
versus NADP+, pH 9.0, 30°C


enzyme_display_name: 4-phosphoerythronate dehydrogenase

proof_lines: in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C

enzyme: 4-phosphoerythronate dehydrogenase


substrate_name: oxaloacetic acid

substrate: oxaloacetic acid


substrate_name: pyruvate

substrate: pyruvate


proof_lines: pH 8.0, 22°C, recombinant enzyme, versus 2-oxoglutarate

proof_lines: pH 8.0, 22°C, recombinant enzyme, versus 4-phospho-D-erythronate


enzyme_display_name: NADP-retinol dehydrogenase

organism: Danio rerio

substrate_name: all-trans-retinal

enzyme: NADP-retinol dehydrogenase

substrate: all-trans-retinal


substrate_name: estrone

substrate: estrone


organism: Drosophila melanogaster

proof_lines: Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines:
membrane-bound wild-type
wild-type

substrate: NADP+


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

proof_lines: pH 7.4, 37°C, determined with all-trans-retinal


assay_conditions_summary: cofactor NADPH


substrate_name: all-trans-retinol

substrate: all-trans-retinol


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines: pH 7.4, 37°C, determined with all-trans-retinol


proof_lines:
37°C
purified recombinant enzyme
pH 7.4, 37°C


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

proof_lines: pH and temperature not specified in the publication. The apparent Km value for NADH is three orders of magnitude higher than that for NADPH


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+


proof_lines:
wild-type
membrane-bound wild-type
wild-type, pH 7.3, 37°C


enzyme_display_name: UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)

substrate_name: UDP-glucuronate

proof_lines: pH 7.5, 30°C, S433A decarboxylase mutant

substrate: UDP-glucuronate


proof_lines: pH 7.5, 30°C, E434A decarboxylase mutant

enzyme: UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


proof_lines: pH 7.5, 30°C, E434A decarboxylase mutant, E434Q decarboxylase mutant


proof_lines:
pH 8.0, 37°C, C-terminal domain of ArnA
pH 8.0, 37°C, full-length enzyme
pH 7.5, 30°C, ArnA decarboxylase domain


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Candida tropicalis

substrate_name: D-xylose

proof_lines: native enzyme; assay note present but not identity-resolving

proof_lines: recombinant enzyme; assay note present but not identity-resolving

enzyme: D-xylose reductase [NAD(P)H]

substrate: D-xylose


substrate_name: NADPH

assay_conditions_summary: pH 5.5; 318.15 K; cofactor NADPH

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

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

substrate: NADPH


assay_conditions_summary: pH 5.5; 318.15 K; cofactor NADH


organism: Rasamsonia emersonii

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADPH

proof_lines: pH 6.5, 37°C, cosubstrate: NADH, wild-type enzyme

proof_lines: pH 6.5, 37°C, cosubstrate: NADPH, wild-type enzyme

proof_lines: wild-type, cosubstrate NADPH, pH 6.5, 37°C


assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH

proof_lines:
wild-type, pH 6.5, 37°C
pH 6.5, 37°C, wild-type enzyme


proof_lines: mutant K271R/N273, cosubstrate NADH, pH 6.5, 37°C

proof_lines: mutant K271R/N273, cosubstrate NADPH, pH 6.5, 37°C


enzyme_display_name: benzil reductase [(S)-benzoin forming]

organism: Bacillus cereus

substrate_name: benzil

enzyme: benzil reductase [(S)-benzoin forming]

substrate: benzil


substrate_name: UDP-N-acetyl-alpha-D-mannosamine

proof_lines: pH 10.0, 37°C, presence of 1 mM N-acetylglucosamine 1-phosphate

substrate: UDP-N-acetyl-alpha-D-mannosamine


substrate_name: NAD+

assay_conditions_summary: pH 10; 310.15 K; cofactor NAD+

substrate: NAD+


organism: Methanococcus maripaludis

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+


enzyme_display_name: 2-dehydropantolactone reductase

organism: Candida orthopsilosis

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

enzyme: 2-dehydropantolactone reductase


organism: Candida parapsilosis

substrate_name: isatin

substrate: isatin


proof_lines:
pH 7.0, 30°C
pH 7.0, 30°C, substrate: isatin


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: glucose-6-phosphate 3-dehydrogenase

organism: Bacillus subtilis

substrate_name: D-glucose 6-phosphate

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

proof_lines: pH 9.5, 25°C, recombinant enzyme NtdC coupled to enzyme NtdA

enzyme: glucose-6-phosphate 3-dehydrogenase

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+


enzyme_display_name: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

organism: Acinetobacter lwoffii

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: oxaloacetate

enzyme: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

substrate: oxaloacetate


substrate_name: L-malate

substrate: L-malate


assay_conditions_summary: cofactor NAD+


organism: Ananas comosus

assay_conditions_summary: pH 7.5; cofactor NADH


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: oxidized isoform cytMDH1, at pH 7.5 and 25°C

proof_lines: reduced isoform cytMDH1, at pH 7.5 and 25°C


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 8; 338.15 K; cofactor NADH

proof_lines: pH and temperature not specified in the publication


substrate_name: (S)-malate

substrate: (S)-malate


organism: Aspergillus niger

proof_lines:
mitochondrial MDH
cyt MDH


proof_lines:
mit MDH
cytosolic MDH


organism: Bos taurus


substrate_name: phenylpyruvate

substrate: phenylpyruvate


organism: Candida albicans

assay_conditions_summary: pH 7.6; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2


organism: Canis lupus familiaris


substrate_name: Indolepyruvate

substrate: Indolepyruvate


organism: Drosophila virilis

proof_lines:
cytoplasmic enzyme
mitochondrial enzyme


organism: Echinococcus granulosus

assay_conditions_summary: pH 8

proof_lines: pH 8.0, recombinant protein fusions with glutathione S-transferase

proof_lines: pH 8.0, recombinant enzyme with a poly-His tail


assay_conditions_summary: pH 8; cofactor NADH

proof_lines: pH 8.0, recombinant enzyme with a poly-His tai


assay_conditions_summary: pH 7.6; cofactor NAD+

proof_lines: pH 7.6, recombinant enzyme with a poly-His tail

proof_lines: pH 7.6, recombinant protein fusions with glutathione S-transferase


proof_lines: pH 7.6, native enzyme, recombinant protein fusions with glutathione S-transferase


organism: Escherichia coli


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

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


organism: Glaesserella parasuis


substrate_name: 3-acetylpyridine adenine dinucleotide

substrate: 3-acetylpyridine adenine dinucleotide


substrate_name: Thionicotinamide adenine dinucleotide

substrate: Thionicotinamide adenine dinucleotide


substrate_name: pyridine 3-aldehyde adenine dinucleotide


substrate_name: nicotinamide hypoxanthine dinucleotide

substrate: nicotinamide hypoxanthine dinucleotide


substrate_name: malate

substrate: malate


organism: Malus domestica

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH


organism: Moritella sp.

proof_lines:
pH 7.0, 30°C, recombinant enzyme
pH 7.0, 30°C


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

proof_lines: enzyme from strain 5710, at pH 7.5 and 30°C


organism: Mycobacterium tuberculosis

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


organism: Phytophthora infestans

proof_lines: recombinant wild type mitochondrial MDH, at 25°C

proof_lines: native wild type mitochondrial MDH, at 25°C

proof_lines: recombinant wild type cytosolic MDH, at 25°C


assay_conditions_summary: 298.15 K; cofactor NADH


assay_conditions_summary: 298.15 K; cofactor NAD+


organism: Rasamsonia emersonii

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NAD+

proof_lines:
pH 7.4, 30°C, native enzyme
pH 7.4, 30°C, recombinant enzyme
native enzyme, at pH 7.4 and 30°C


proof_lines:
pH 7.4, 30°C, native enzyme
pH 7.4, 30°C, recombinant enzyme


proof_lines:
pH 7.4, 30°C, recombinant enzyme
pH 7.4, 30°C, native enzyme
native enzyme, at pH 7.4 and 30°C


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH


organism: Rattus norvegicus

proof_lines:
normal rats
ischemic rats


assay_conditions_summary: cofactor NADH


organism: Rhodopseudomonas palustris

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines:
pH 8.0, 25°C, tetrameric enzyme form
pH 8.0, 25°C, dimeric enzyme form


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines:
pH 9.0, 25°C, dimeric enzyme form
pH 9.0, 25°C, tetrameric enzyme form


organism: Saccharomyces cerevisiae

proof_lines: fusion protein of MDH with mitochondrial citrate synthase

proof_lines: in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2


assay_conditions_summary: cofactor NAD+


organism: Salinibacter ruber

assay_conditions_summary: pH 8; 333.15 K; cofactor NADH


organism: Spinacia oleracea

proof_lines:
chloroplast envelope enzyme fraction
plasma membrane-bound enzyme fraction
chloroplast stroma enzyme fraction


enzyme_display_name: leucine dehydrogenase

organism: Geobacillus stearothermophilus

substrate_name: L-norvaline

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

enzyme: leucine dehydrogenase

substrate: L-norvaline


substrate_name: L-norleucine

smiles: CCCCC(C(=O)O)N

substrate: L-norleucine


substrate_name: L-Ile

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

substrate: L-Ile


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


enzyme_display_name: glucokinase

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: glucokinase

substrate: ATP


enzyme_display_name: aspartate 1-decarboxylase

organism: Pyrococcus furiosus

substrate_name: L-Aspartate

source_db: oed

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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

data_origin: experimental

enzyme: aspartate 1-decarboxylase

substrate: L-Aspartate

source: oed


enzyme_display_name: Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase

organism: Comamonas testosteroni

substrate_name: L-aspartate

source_db: uniprot

substrate: L-aspartate

source: uniprot


enzyme_display_name: UniProt P69910

substrate_name: L-glutamate

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P69910

substrate: L-glutamate

source: skid


enzyme_display_name: glutamate decarboxylase

enzyme: glutamate decarboxylase


enzyme_display_name: aspartate 4-decarboxylase

organism: [Pseudomonas] dacunhae

enzyme: aspartate 4-decarboxylase


organism: Alcaligenes faecalis

substrate_name: erythro-beta-hydroxyaspartate

substrate: erythro-beta-hydroxyaspartate


substrate_name: threo-beta-hydroxyaspartate

substrate: threo-beta-hydroxyaspartate


substrate_name: L-Asp

substrate: L-Asp


substrate_name: aminomalonate

substrate: aminomalonate


organism: Acinetobacter radioresistens

proof_lines: mutant K18A/V287I, pH not specified in the publication temperature not specified in the publication


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


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


substrate_name: L-alanine

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

substrate: L-alanine


organism: Lactiplantibacillus plantarum subsp. plantarum


substrate_name: L-Glutamate; 4-Aminobutanoate; CO2

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

substrate: L-Glutamate; 4-Aminobutanoate; CO2


substrate_name: L-Glutamate; CO2; 4-Aminobutanoate

substrate: L-Glutamate; CO2; 4-Aminobutanoate


organism: Aedes aegypti


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


proof_lines: mutant E88R, 23°C, pH not specified in the publication


organism: Pseudomonas dacunhae

proof_lines: in presence of 2-oxoglutarate or pyridoxal 5'-phosphate


proof_lines: mutant enzyme R37A, in 50 mM potassium phosphate, at pH 7.0 and 37°C


proof_lines: wild type enzyme, in 50 mM potassium phosphate, at pH 7.0 and 37°C


organism: Cunninghamella elegans


assay_conditions_summary: pH 7; 298.15 K; buffer 0.2 M phosphate

proof_lines: in 0.2 M phosphate buffer (pH 7.0) containing 0.1 mM pyridoxal 5'-phosphate, at 25°C


organism: Mycobacterium tuberculosis


organism: Penicillium citrinum


organism: Rattus norvegicus

proof_lines:
brain enzyme
liver and kidney enzyme


enzyme_display_name: malonyl-CoA decarboxylase

organism: Aix sponsa

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: malonyl-CoA decarboxylase

substrate: malonyl-CoA


organism: Anser domesticus


organism: Branta leucopsis


organism: Anopheles gambiae

assay_conditions_summary: pH 7; buffer 0.2 M phosphate


organism: Saccharopolyspora erythraea

substrate_name: N-hydroxy-L-ornithine

proof_lines: in 20 mM Tris, 100 mM NaCl, pH 7.2, at 25°C

substrate: N-hydroxy-L-ornithine


organism: Corynebacterium jeikeium

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4JXL3 and applied mutation signature A74G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM HEPES

column_label: Table 2: Kinetic and inactivation parameters of wild-type PanD and its variants (World Journal of Microbiology and Biotechnology 2019, 35:62); printed column heads Mutants no. | Mutation sites | Activity (umol/min/mL) | Km (mM) | kcat (/s) | kcat/Km | kobs x 10^-3 (/min). Table 2, Mutants no. row A24, Mutation sites A74G; column Mutants no. = A24; column Mutation sites = A74G; column Activity (umol/min/mL) = 16.54; column Km (mM) = 3.15; column kcat (/s) = 6.73; column kcat/Km = 2.14; column kobs x 10^-3 (/min) = 7.25. captured primary segment: mutant no. A24 | mutation site A74G | Activity 16.54 umol/min/mL | Km 3.15 mM | kcat 6.73 s^-1 | kcat/Km 2.14 s^-1 mM^-1 | kobs 7.25 x 10^-3 min^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.73 under the column head kcat (/s); that unit is s^-1, which is already canonical, so no unit conversion applies and the value is 6.73 s^(-1). Km: printed Table 2 cell 3.15 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 3.15 mM. kcat/Km: printed Table 2 cell 2.14 under a column head that carries no unit of its own; the unit implied by the Km (mM) and kcat (/s) heads beside it is s^-1 mM^-1, which is already canonical, so no unit conversion applies and the paper-side value is 2.14 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.73 / 3.15 = 2.136507936507937 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.14 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Mutants no. row A24 with Mutation sites A74G: Km = 3.15 mM; kcat = 6.73 s^-1; printed kcat/Km = 2.14 s^-1 mM^-1.

status: verified


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

assay_conditions_summary: pH 7


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4JXL3 and applied mutation signature E42Q to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic and inactivation parameters of wild-type PanD and its variants (World Journal of Microbiology and Biotechnology 2019, 35:62); printed column heads Mutants no. | Mutation sites | Activity (umol/min/mL) | Km (mM) | kcat (/s) | kcat/Km | kobs x 10^-3 (/min). Table 2, Mutants no. row E68, Mutation sites E42Q; column Mutants no. = E68; column Mutation sites = E42Q; column Activity (umol/min/mL) = 17.98; column Km (mM) = 1.66; column kcat (/s) = 6.77; column kcat/Km = 4.07; column kobs x 10^-3 (/min) = 10.16. captured primary segment: mutant no. E68 | mutation site E42Q | Activity 17.98 umol/min/mL | Km 1.66 mM | kcat 6.77 s^-1 | kcat/Km 4.07 s^-1 mM^-1 | kobs 10.16 x 10^-3 min^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.77 under the column head kcat (/s); that unit is s^-1, which is already canonical, so no unit conversion applies and the value is 6.77 s^(-1). Km: printed Table 2 cell 1.66 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 1.66 mM. kcat/Km: printed Table 2 cell 4.07 under a column head that carries no unit of its own; the unit implied by the Km (mM) and kcat (/s) heads beside it is s^-1 mM^-1, which is already canonical, so no unit conversion applies and the paper-side value is 4.07 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.77 / 1.66 = 4.078313253012048 s^-1 mM^-1, against the printed catalytic-efficiency cell 4.07 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Mutants no. row E68 with Mutation sites E42Q: Km = 1.66 mM; kcat = 6.77 s^-1; printed kcat/Km = 4.07 s^-1 mM^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4JXL3 and applied mutation signature E42D to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic and inactivation parameters of wild-type PanD and its variants (World Journal of Microbiology and Biotechnology 2019, 35:62); printed column heads Mutants no. | Mutation sites | Activity (umol/min/mL) | Km (mM) | kcat (/s) | kcat/Km | kobs x 10^-3 (/min). Table 2, Mutants no. row E71, Mutation sites E42D; column Mutants no. = E71; column Mutation sites = E42D; column Activity (umol/min/mL) = 19.98; column Km (mM) = 0.99; column kcat (/s) = 6.88; column kcat/Km = 6.96; column kobs x 10^-3 (/min) = 9.55. captured primary segment: mutant no. E71 | mutation site E42D | Activity 19.98 umol/min/mL | Km 0.99 mM | kcat 6.88 s^-1 | kcat/Km 6.96 s^-1 mM^-1 | kobs 9.55 x 10^-3 min^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.88 under the column head kcat (/s); that unit is s^-1, which is already canonical, so no unit conversion applies and the value is 6.88 s^(-1). Km: printed Table 2 cell 0.99 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.99 mM. kcat/Km: printed Table 2 cell 6.96 under a column head that carries no unit of its own; the unit implied by the Km (mM) and kcat (/s) heads beside it is s^-1 mM^-1, which is already canonical, so no unit conversion applies and the paper-side value is 6.96 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.88 / 0.99 = 6.94949494949495 s^-1 mM^-1, against the printed catalytic-efficiency cell 6.96 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Mutants no. row E71 with Mutation sites E42D: Km = 0.99 mM; kcat = 6.88 s^-1; printed kcat/Km = 6.96 s^-1 mM^-1.


column_label: Table 2: Kinetic and inactivation parameters of wild-type PanD and its variants (World Journal of Microbiology and Biotechnology 2019, 35:62); printed column heads Mutants no. | Mutation sites | Activity (umol/min/mL) | Km (mM) | kcat (/s) | kcat/Km | kobs x 10^-3 (/min). Table 2, Mutants no. row Wild type, the wild-type row (Mutation sites cell empty); column Mutants no. = Wild type; column Mutation sites = (empty, wild type); column Activity (umol/min/mL) = 16.03; column Km (mM) = 3.31; column kcat (/s) = 6.92; column kcat/Km = 2.09; column kobs x 10^-3 (/min) = 9.37. captured primary segment: mutant no. Wild type | mutation site none (wild type) | Activity 16.03 umol/min/mL | Km 3.31 mM | kcat 6.92 s^-1 | kcat/Km 2.09 s^-1 mM^-1 | kobs 9.37 x 10^-3 min^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.92 under the column head kcat (/s); that unit is s^-1, which is already canonical, so no unit conversion applies and the value is 6.92 s^(-1). Km: printed Table 2 cell 3.31 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 3.31 mM. kcat/Km: printed Table 2 cell 2.09 under a column head that carries no unit of its own; the unit implied by the Km (mM) and kcat (/s) heads beside it is s^-1 mM^-1, which is already canonical, so no unit conversion applies and the paper-side value is 2.09 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.92 / 3.31 = 2.090634441087613 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.09 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Mutants no. row Wild type (the wild-type row): Km = 3.31 mM; kcat = 6.92 s^-1; printed kcat/Km = 2.09 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4JXL3 and applied mutation signature R3K to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic and inactivation parameters of wild-type PanD and its variants (World Journal of Microbiology and Biotechnology 2019, 35:62); printed column heads Mutants no. | Mutation sites | Activity (umol/min/mL) | Km (mM) | kcat (/s) | kcat/Km | kobs x 10^-3 (/min). Table 2, Mutants no. row R53, Mutation sites R3K; column Mutants no. = R53; column Mutation sites = R3K; column Activity (umol/min/mL) = 21.29; column Km (mM) = 1.44; column kcat (/s) = 9.40; column kcat/Km = 6.54; column kobs x 10^-3 (/min) = 3.15. captured primary segment: mutant no. R53 | mutation site R3K | Activity 21.29 umol/min/mL | Km 1.44 mM | kcat 9.40 s^-1 | kcat/Km 6.54 s^-1 mM^-1 | kobs 3.15 x 10^-3 min^-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.40 under the column head kcat (/s); that unit is s^-1, which is already canonical, so no unit conversion applies and the value is 9.4 s^(-1). Km: printed Table 2 cell 1.44 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 1.44 mM. kcat/Km: printed Table 2 cell 6.54 under a column head that carries no unit of its own; the unit implied by the Km (mM) and kcat (/s) heads beside it is s^-1 mM^-1, which is already canonical, so no unit conversion applies and the paper-side value is 6.54 s^(-1)*mM^(-1). Quotient disclosure for this row: 9.40 / 1.44 = 6.527777777777779 s^-1 mM^-1, against the printed catalytic-efficiency cell 6.54 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Mutants no. row R53 with Mutation sites R3K: Km = 1.44 mM; kcat = 9.40 s^-1; printed kcat/Km = 6.54 s^-1 mM^-1.


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E302G with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; cofactor CoA

proof_lines: pH 8.5, temperature not specified in the publication, mutant E302G, no H2O2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C243S with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: pH 8.5, temperature not specified in the publication, mutant C243S, no H2O2

proof_lines: pH 8.5, temperature not specified in the publication, mutant C243S, 0.1 M H2O2

proof_lines: pH 8.5, temperature not specified in the publication, mutant C243S, 0.2 M H2O2


proof_lines: pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.2 M H2O2

proof_lines: pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.05 M H2O2

proof_lines: pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.1 M H2O2


proof_lines: pH 8.5, temperature not specified in the publication, mutant C206S, 0.2 M H2O2

proof_lines: pH 8.5, temperature not specified in the publication, mutant C206S, no H2O2

proof_lines: pH 8.5, temperature not specified in the publication, mutant C206S, 00.1 M H2O2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C206S/C243S to reconstruct the assayed variant sequence.

proof_lines: pH 8.5, temperature not specified in the publication, mutant C206S/C243S, no H2O2

proof_lines: pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.2 M H2O2

proof_lines: pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.1 M H2O2


organism: Mus musculus

proof_lines: kcat is 3.6 sec(-1) with 3-sulfino-L-alanine (cysteine sulfinic acid) as substrate. kcat 1.3 sec(-1) is with L-aspartate as substrate.


proof_lines: kcat is 6.6 sec(-1) with 3-sulfino-L-alanine (cysteine sulfinic acid) as substrate. kcat is 0.14 sec(-1) with L-aspartate as substrate.


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

assay_conditions_summary: pH 8

column_label: Table 1 row L-aspartate column Km (mM) has cell 1.2 +/- 0.1 mM.

raw_value_unit_evidence: Km raw_value=1.2 +/- 0.1 raw_unit=mM

row_label: L-aspartate

table_label: Table 1. Substrate Specificity of PhGAD from P. horikoshii


column_label: Table 1 row L-glutamate column Km (mM) has cell 3.9 +/- 0.4 mM.

raw_value_unit_evidence: Km raw_value=3.9 +/- 0.4 raw_unit=mM

row_label: L-glutamate


substrate_name: cysteate

column_label: Table 1 row Cysteate column Km (mM) has cell 2.2 +/- 0.3 mM.

raw_value_unit_evidence: Km raw_value=2.2 +/- 0.3 raw_unit=mM

row_label: Cysteate

substrate: cysteate


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

substrate_name: aspartate

proof_lines: kcat is 0.80 sec(-1) with aspartate as substrate. kcat is 0.18 sec(-1) with glutamate as substrate.

substrate: aspartate


substrate_name: glutamate

substrate: glutamate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.65 sec(-1), specific activity 2100 nmol/min/mg for L-aspartate.


organism: Pseudomonas sp.

source_databases_merged: brenda uniprot


organism: Aliivibrio fischeri (strain ATCC 700601 / ES114)

substrate_name: aspartate (at 28 degrees Celsius)

proof_lines: kcat is 0.075 sec(-1) at 28 degrees Celsius. kcat is 0.008 sec(-1) at 37 degrees Celsius.

substrate: aspartate (at 28 degrees Celsius)


substrate_name: glutamate (at 37 degrees Celsius)

proof_lines: kcat is 0.055 sec(-1) at 37 degrees Celsius.

substrate: glutamate (at 37 degrees Celsius)


substrate_name: Malonyl-CoA

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

sequence_source: multiple

proof_lines: pH and temperature not specified in the publication

proof_lines: kcat is 19 sec(-1) with malonyl-CoA for malonyl-CoA decarboxylase mitochondrial form (PubMed:15003260). kcat is 28 sec(-1) with malonyl-CoA for Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form (PubMed:15003260). The catalytic efficien

source_databases_merged: sabio_rk brenda skid uniprot

substrate: Malonyl-CoA


mutation_signature: full-length and N-terminal truncated apo-hMCD full-length and N-terminal truncated apo-hMCD

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

mutation_type: truncation


organism: Brucella microti

assay_conditions_summary: pH 4.6; 298.15 K; buffer 50 mM sodium acetate


substrate_name: L-Glu

proof_lines: GAD65 after cleavage with protease factor Xa

proof_lines: GAD65-GST fusion protein expressed in Escherichia coli

substrate: L-Glu


organism: Latilactobacillus sakei

substrate_name: L-glutamate

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

column_label: PubMed abstract reports: The Km and Vmax of GAD were 0.045 mM and 0.011 mM/min, respectively, when glutamate was used as the substrate.

raw_value_unit_evidence: Km raw_value=0.045 mM raw_unit=mM

row_label: Purified Lactobacillus sakei GAD / glutamate

table_label: PubMed XML abstract PMID 25791853

substrate: L-glutamate


organism: Levilactobacillus senmaizukei

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


organism: Bos taurus

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

proof_lines:
in presence of 150 mM PO43-
in presence of 40 mM PO43-


organism: Rattus norvegicus

sequence: MRGLGPSLRARRLLPLRYPPR

wild_type_sequence: MRGLGPSLRARRLLPLRYPPR

assay_conditions_summary: pH 7; cofactor CoA

column_label: Abstract reports recombinant rat malonyl-CoA decarboxylase showed Michaelis-Menten saturation and Km was calculated to be 68 microM.

raw_value_unit_evidence: Km raw_value=68 microM raw_unit=microM

row_label: Rat malonyl-CoA decarboxylase / malonyl-CoA

table_label: PubMed XML abstract PMID 12297032


organism: Synechocystis sp. PCC 6803


organism: Levilactobacillus brevis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K17T/D294G/E312S/Q346H to reconstruct the assayed variant sequence.

proof_lines: C-terminal truncation mutant K17T/D294G/E312S/Q346H, pH not specified in the publication, temperature not specified in the publication


substrate_name: cysteine sulfite

column_label: Table 1 row Cysteine sulfite column Km (mM) has cell 32.6 +/- 5.4 mM.

raw_value_unit_evidence: Km raw_value=32.6 +/- 5.4 raw_unit=mM

row_label: Cysteine sulfite

substrate: cysteine sulfite


substrate_name: Unknown

substrate: Unknown


proof_lines: kcat is 0.34 sec(-1) with L-aspartate as substrate. kcat is 0.26 sec(-1) with L-glutamate as substrate. kcat is 0.65 sec(-1) with cysteate as substrate. kcat is 0.03 sec(-1) with cysteine sulfite as substrate.


proof_lines: pH 7.3, 25°C, GAD65, recombinant enzyme expressed in Escherichia coli


organism: Bacillus subtilis

substrate_name: L-Aspartate

sequence_variant_note: Mutation signature I188M references residue 188, which is outside the resolved sequence length.

proof_lines:
L-aspartate-α-decarboxylase
specific activity
thermostability

substrate: L-Aspartate


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


substrate_name: 3-sulfino-L-alanine (cysteine sulfinic acid)


organism: Escherichia coli

proof_lines:
aspartate alpha-decarboxylase
Escherichia coli
L-aspartate

source_databases_merged: sabio_rk brenda uniprot


enzyme_display_name: ornithine decarboxylase

organism: Lactobacillus sp. 30a

substrate_name: alpha-Methylornithine

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

enzyme: ornithine decarboxylase

substrate: alpha-Methylornithine


enzyme_display_name: Lysine/ornithine decarboxylase

organism: Selenomonas ruminantium

substrate_name: L-lysine

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

enzyme: Lysine/ornithine decarboxylase

substrate: L-lysine


enzyme_display_name: UniProt P0A9H3

proof_lines:
Raw SKiD Env: Temp=10°C, pH=6.5
Raw SKiD Env: Temp=45°C, pH=5.6

enzyme: UniProt P0A9H3


substrate_name: L-ornithine

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

substrate: L-ornithine


enzyme_display_name: UniProt P9WIU7

organism: Mycobacterium tuberculosis

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.8
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P9WIU7


enzyme_display_name: UniProt Q73PV9

organism: Treponema denticola

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=10°C, pH=8

enzyme: UniProt Q73PV9


substrate_name: 5-aminoimidazole ribonucleotide

substrate: 5-aminoimidazole ribonucleotide


enzyme_display_name: histidine decarboxylase

organism: Staphylococcus epidermidis

substrate_name: L-histidine

enzyme: histidine decarboxylase

substrate: L-histidine


enzyme_display_name: UniProt O26232

organism: Methanothermobacter thermautotrophicus

substrate_name: orotidine 5'-phosphate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.1

enzyme: UniProt O26232

substrate: orotidine 5'-phosphate


enzyme_display_name: UniProt Q8IJH3

organism: Plasmodium falciparum

enzyme: UniProt Q8IJH3


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H465A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


substrate_name: L-Glutamate

substrate: L-Glutamate


organism: Methanocaldococcus jannaschii

substrate_name: L-aspartate

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

source_databases_merged: skid uniprot

substrate: L-aspartate


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

substrate_name: L-tyrosine

column_label: The ScienceDirect full text states that the enzyme had a specific activity for the decarboxylation of L-tyrosine of 1.1 (+/- 0.12) U mg-1 protein with a Km of 1.6 (+/- 0.29) mM.

raw_value_unit_evidence: Km raw_value=1.6 raw_unit=mM

row_label: Methanocaldococcus jannaschii MfnA / L-tyrosine

table_label: ScienceDirect full text PMID 15715981 MfnA enzyme characterization prose

substrate: L-tyrosine


organism: Brucella microti


organism: Achromobacter sp.

substrate_name: L-Asp

proof_lines:
l-aspartate 4-carboxy-lyase
Achromobacter sp.

substrate: L-Asp


organism: Homo sapiens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q5D/V6I/T7E to reconstruct the assayed variant sequence.


organism: Lacticaseibacillus paracasei

column_label: Abstract reports Km value for glutamate was 5.0 mM.

raw_value_unit_evidence: Km raw_value=5.0 mM raw_unit=mM

row_label: Lactobacillus paracasei NFRI 7415 GAD / L-glutamate

table_label: PubMed XML abstract PMID 18256502


organism: Rattus norvegicus

substrate_name: Malonyl-CoA


organism: Comamonas testosteroni

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


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


organism: Synechocystis sp. PCC 6803

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

column_label: PubMed abstract for PMID 26730883 reports catalytic properties for the enzyme: Km 19.6 mM, kcat 100.7 s(-1), and kcat/Km 5.1 mM(-1) s(-1).

normalized_value_unit_evidence: Km normalized_value=19.6 normalized_unit=mM; kcat normalized_value=100.7 normalized_unit=s^-1; kcat/Km paper rounded normalized_value=5.1 normalized_unit=s^-1*mM^-1; exported central ratio 100.7/19.6=5.137755102040816 s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=19.6 raw_unit=mM; kcat raw_value=100.7 raw_unit=s^-1; kcat/Km printed raw_value=5.1 raw_unit=mM^-1 s^-1.

row_label: Synechocystis sp. PCC6803 glutamate decarboxylase / L-glutamate

table_label: PubMed XML abstract PMID 26730883


organism: Cairina moschata

substrate_name: malonyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

column_label: PMID 102255 DOI 10.1016/0003-9861(78)90314-4 Table I; row Muscovy duck; column Malonyl-CoA Km (uM).

raw_value_unit_evidence: Table I row Muscovy duck: Malonyl-CoA Km 32 uM; supporting prose gives 32 uM and V 75 umol/min/mg for the muscovy duck enzyme.

row_label: Muscovy duck (Cairina moschatta / Cairina moschata)

table_label: Table I. Malonyl-CoA decarboxylase content and fatty acid composition of the uropygial glands of geese and ducks and Michaelis-Menten constants of the enzymes from these glands

substrate: malonyl-CoA


organism: Levilactobacillus brevis

substrate_name: L-glutamate


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


organism: Bacillus subtilis


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


organism: Escherichia coli

assay_conditions_summary: pH 4.6; 310.15 K; buffer 0.2 M pyridine/HCl

proof_lines: mutant enzyme DELTAHT, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C


proof_lines: mutant enzyme H465A, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C


proof_lines: wild type enzyme, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C

proof_lines: pH 4.6, 37°C, recombinant C-terminally His-tagged wild-type enzyme

proof_lines: pH 4.6, 37°C, recombinant untagged wild-type enzyme


organism: Bos taurus

substrate_name: L-Glu

proof_lines: from pH 5.8 to pH 7.8 the Km decreases from 1.7 mM at pH 5.8 to 0.5 mM at pH 7.8


substrate_name: cysteine sulfinic acid

substrate: cysteine sulfinic acid


substrate_name: L-cysteic acid

substrate: L-cysteic acid


organism: Priestia megaterium

proof_lines: recombinant wild-type enzyme, pH 5.0, 50°C

substrate: L-glutamate


proof_lines: mutant with N-terminal deletion of 90 amino acids, pH 7.2


proof_lines: mutant with N-terminal deletion of 70 amino acids, pH 7.2


organism: Lactiplantibacillus plantarum subsp. plantarum

proof_lines: pH 5.0, 37°C, recombinant wild-type enzyme


proof_lines: pH 7.0, 37°C, recombinant enzyme mutant DELTA11

proof_lines: pH 5.0, 37°C, recombinant enzyme mutant DELTA11


organism: Lactiplantibacillus plantarum

assay_conditions_summary: pH 5

proof_lines: wild-type, pH 5, temperature not specified in the publication


mutation_signature: C-terminal trunction mutant

proof_lines: C-terminal trunction mutant, pH 5, temperature not specified in the publication


mutation_signature: Δ1

proof_lines: pH 4.6, 37°C, recombinant deletion mutant GadBDELTA1-14


proof_lines: pH 4.6, 37°C, recombinant mutant Q5D/V6I/T7E


organism: Priestia aryabhattai


organism: Tribolium castaneum

proof_lines:
wild-type, pH 7, 37°C
wild-type, pH 6.5, 37°C


organism: Alcaligenes sp.


organism: Anas platyrhynchos


organism: Anser sp.


organism: Aspergillus oryzae

substrate: L-Glu


organism: Bacillus

proof_lines:
isoform GadZ20, pH 5.0, 40°C
isoform GadZ1, pH 5.0, 40°C
isoform GadZ11, pH 5.0, 40°C


organism: Camellia sinensis


organism: Clostridium perfringens


organism: Ctenocephalides felis


organism: Cucurbita maxima


organism: Drosophila melanogaster


organism: Enterococcus avium

proof_lines: pH 5.5, 45°C, recombinant His-tagged enzyme


organism: Enterococcus faecium


organism: Enterococcus raffinosus


organism: Escherichia coli


substrate_name: L-alpha-Methylglutamate

substrate: L-alpha-Methylglutamate


organism: Felis catus


organism: Homo sapiens

proof_lines: GAD67 after cleavage with protease factor Xa

proof_lines: GAD67-GST fusion protein expressed in Escherichia coli

proof_lines: isoform GAD67, lacking aminoterminal 70 amino acids, presence of apocalmodulin


substrate_name: Unknown

proof_lines: pH 7.3, 25°C, GAD67, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 7.3, 25°C, GAD56, recombinant enzyme expressed in Escherichia coli

substrate: Unknown


enzyme_display_name: UniProt Q8RY79

organism: Arabidopsis thaliana

substrate_name: L-phenylalanine

enzyme: UniProt Q8RY79

substrate: L-phenylalanine


enzyme_display_name: tyrosine decarboxylase

organism: Pyrococcus furiosus

enzyme: tyrosine decarboxylase


enzyme_display_name: UniProt Q88JU5

organism: Pseudomonas putida

substrate_name: L-Dopa

enzyme: UniProt Q88JU5

substrate: L-Dopa


enzyme_display_name: UniProt P00864

substrate_name: phosphoenolpyruvate

enzyme: UniProt P00864

substrate: phosphoenolpyruvate


enzyme_display_name: Phosphoenolpyruvate carboxylase

organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

enzyme: Phosphoenolpyruvate carboxylase


enzyme_display_name: UniProt P21642

organism: Gallus gallus

substrate_name: GDP

enzyme: UniProt P21642

substrate: GDP


enzyme_display_name: UniProt P35558

enzyme: UniProt P35558


enzyme_display_name: glutamate decarboxylase

organism: Hordeum vulgare

enzyme: glutamate decarboxylase


organism: Levilactobacillus brevis

assay_conditions_summary: pH 5.2; 318.15 K; buffer acetate

proof_lines:
pH 5.2, 45°C, recombinant enzyme
pH 4.6, 37°C, native enzyme
pH 4.6, 37°C, recombinant enzyme


proof_lines: C-terminal truncation mutant lacking 11 amino acids, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: aspartate 1-decarboxylase

organism: Methanocaldococcus jannaschii

enzyme: aspartate 1-decarboxylase


organism: Mus musculus


organism: Monascus purpureus


organism: Mycobacterium tuberculosis


organism: Photobacterium damselae subsp. piscicida


organism: Oryza sativa

proof_lines:
partially purified enzyme, pH 5.6, 40°C
pH 5.6, 40°C


organism: Neurospora crassa


organism: Priestia aryabhattai


enzyme_display_name: malonyl-CoA decarboxylase

organism: Rattus norvegicus

assay_conditions_summary: pH 8.5; 333.15 K; buffer 100 mM potassium phosphate; cofactor CoA

proof_lines: gastrocnemius after 5 min of contraction

proof_lines: in 100 mM potassium phosphate buffer (pH 8.5) and 1 mM thiophenol, at 60°C

enzyme: malonyl-CoA decarboxylase


organism: Rhizobium leguminosarum


proof_lines: isoform GAD67, treated with trypsin, which also increases vmax value by 31%

proof_lines: isoform GAD65, treated with trypsin, which also increases vmax value by 33%


organism: Saccharomyces cerevisiae


organism: Solanum tuberosum


organism: Sus scrofa

proof_lines:
enzyme form alpha
enzyme form beta
gamma-form


organism: Streptococcus thermophilus


organism: Tribolium castaneum


organism: Vicia faba


organism: Vigna unguiculata


organism: Corynebacterium jeikeium


enzyme_display_name: UniProt P32377

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

enzyme: UniProt P32377


enzyme_display_name: UniProt Q9FD73

organism: Staphylococcus epidermidis

enzyme: UniProt Q9FD73


substrate_name: ATP

substrate: ATP


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


enzyme_display_name: UDP-glucuronate decarboxylase

organism: Papiliotrema laurentii

substrate_name: UDPglucuronate

enzyme: UDP-glucuronate decarboxylase

substrate: UDPglucuronate


enzyme_display_name: UniProt P06132

organism: Homo sapiens

substrate_name: uroporphyrinogen-III

enzyme: UniProt P06132

substrate: uroporphyrinogen-III


substrate_name: uroporphyrinogen-I

substrate: uroporphyrinogen-I


enzyme_display_name: ribulose-bisphosphate carboxylase

organism: Paracoccus denitrificans

enzyme: ribulose-bisphosphate carboxylase


substrate_name: D-ribulose 1,5-bisphosphate

substrate: D-ribulose 1,5-bisphosphate


enzyme_display_name: UniProt O93627

organism: Thermococcus kodakarensis

enzyme: UniProt O93627


enzyme_display_name: UniProt P04718

organism: Rhodospirillum rubrum

smiles: O=O

enzyme: UniProt P04718


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


enzyme_display_name: UniProt O28635

organism: Archaeoglobus fulgidus

proof_lines:
Raw SKiD Env: Temp=83°C, pH=-----
Raw SKiD Env: Temp=83°C, pH=8.3

enzyme: UniProt O28635


enzyme_display_name: Ribulose bisphosphate carboxylase large chain

organism: Hydrogenophaga pseudoflava

substrate_name: ribulose 1,5-bisphosphate

substrate: ribulose 1,5-bisphosphate


smiles: [Co]

enzyme: Ribulose bisphosphate carboxylase large chain


organism: Xanthobacter flavus

smiles: O=C=O


substrate_name: D-Ribulose 1,5-bisphosphate; H2O; CO2

substrate: D-Ribulose 1,5-bisphosphate; H2O; CO2


organism: Zea mays

substrate_name: H2O; CO2; D-Ribulose 1,5-bisphosphate

substrate: H2O; CO2; D-Ribulose 1,5-bisphosphate


organism: Bradyrhizobium diazoefficiens


substrate_name: CO2; H2O; D-Ribulose 1,5-bisphosphate

substrate: CO2; H2O; D-Ribulose 1,5-bisphosphate


organism: Nicotiana tabacum

substrate_name: CO2; D-Ribulose 1,5-bisphosphate; H2O

substrate: CO2; D-Ribulose 1,5-bisphosphate; H2O


substrate_name: D-Ribulose 1,5-bisphosphate; CO2; H2O

substrate: D-Ribulose 1,5-bisphosphate; CO2; H2O


substrate_name: H2O; D-Ribulose 1,5-bisphosphate; CO2

substrate: H2O; D-Ribulose 1,5-bisphosphate; CO2


organism: Rhodobacter sphaeroides


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L341M to reconstruct the assayed variant sequence.


enzyme_display_name: diphosphomevalonate decarboxylase

organism: Cymbopogon citratus

enzyme: diphosphomevalonate decarboxylase


substrate_name: GTP

substrate: GTP


substrate_name: CTP

substrate: CTP


organism: Thiomicrospira thyasirae


organism: Equus caballus


organism: Synechococcus sp.

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


substrate_name: D-Ribulose 1,5-bisphosphate

substrate: D-Ribulose 1,5-bisphosphate


organism: Synechococcus elongatus


organism: Gossypium hirsutum


substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Rattus norvegicus


substrate_name: phosphopantothenoyl-L-Cys

substrate: phosphopantothenoyl-L-Cys


organism: Acinetobacter sp.


organism: Aphanothece halophytica


organism: Lolium giganteum

proof_lines: 20°C, pH not specified in the publication

proof_lines: 25°C, pH not specified in the publication

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


organism: Selenomonas ruminantium

substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


organism: Helianthus tuberosus

substrate_name: UDPglucuronate

substrate: UDPglucuronate


organism: Lemna minor


organism: Oryctolagus cuniculus


organism: Flavobacterium johnsoniae


organism: Sus scrofa


enzyme_display_name: uroporphyrinogen decarboxylase

organism: Homo sapiens

substrate_name: 5-COOH-porphyrinogen III

proof_lines:
isoenzyme I
isoenzyme II
enzyme from healthy individuals

enzyme: uroporphyrinogen decarboxylase

substrate: 5-COOH-porphyrinogen III


organism: Neohelice granulata


organism: Parachlorella kessleri

substrate_name: uroporphyrinogen III

substrate: uroporphyrinogen III


organism: Sorghum bicolor


organism: Eucalyptus moorei

substrate_name: D-ribulose 1,5-bisphosphate

proof_lines: in 100 mM Bicine-NaOH pH 8.0, 20 mM MgCl2, at 25°C

substrate: D-ribulose 1,5-bisphosphate


organism: Aphanocapsa alpicola


organism: Eucalyptus neglecta


organism: Panicum milioides


organism: Plectonema boryanum


organism: Helianthus maximus


organism: Anaerolinea thermophila

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R71A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R26V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N20K/H194M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N20K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H194M to reconstruct the assayed variant sequence.


substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P54205 and applied mutation signature H298A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic properties of Rubisco mutants), strain row 'H298A'; column 'Site' = 5P; column 'Kcat (min-1)' = 43; column 'Km(RuBP) (uM)' = 267; column 'apparent Km (CO2) (uM)' = NM; column 'Ki(Pi) (mM)' = 6.3. Table 2 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 43 under the column head Kcat (min-1); one min^-1 is 1/60 s^-1, so 43 / 60 = 0.7166666666666667 s^(-1). km: printed Table 2 cell 267 under the column head Km(RuBP) (uM); one uM is 1/1000 mM, so 267 / 1000 = 0.267 mM. kcat/Km: Table 2 has no kcat/Km column, so nothing is converted for the ratio; the canonical catalytic efficiency is the quotient of those two converted cells of the same strain row, 0.7166666666666667 / 0.267 = 2.6841448189762795 s^(-1)*mM^(-1), typed derived_same_measurement against them.

raw_value_unit_evidence: Table 2, strain row H298A, site 5P: Kcat = 43 min^-1; Km(RuBP) = 267 uM. Table 2 prints no kcat/Km column, and this article prints no catalytic-efficiency cell for this measurement.

row_label: Table 2, strain row H298A, site 5P

table_label: Table 2: Kinetic properties of Rubisco mutants (Journal of Bacteriology 2005, 187(12):4222-4228)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P54205 and applied mutation signature H327Q with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic properties of Rubisco mutants), strain row 'H327Q'; column 'Site' = 5P; column 'Kcat (min-1)' = 92; column 'Km(RuBP) (uM)' = 490; column 'apparent Km (CO2) (uM)' = 175; column 'Ki(Pi) (mM)' = 0.67. Table 2 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 92 under the column head Kcat (min-1); one min^-1 is 1/60 s^-1, so 92 / 60 = 1.5333333333333334 s^(-1). km: printed Table 2 cell 490 under the column head Km(RuBP) (uM); one uM is 1/1000 mM, so 490 / 1000 = 0.49 mM. kcat/Km: Table 2 has no kcat/Km column, so nothing is converted for the ratio; the canonical catalytic efficiency is the quotient of those two converted cells of the same strain row, 1.5333333333333334 / 0.49 = 3.1292517006802725 s^(-1)*mM^(-1), typed derived_same_measurement against them.

raw_value_unit_evidence: Table 2, strain row H327Q, site 5P: Kcat = 92 min^-1; Km(RuBP) = 490 uM. Table 2 prints no kcat/Km column, and this article prints no catalytic-efficiency cell for this measurement.

row_label: Table 2, strain row H327Q, site 5P


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K305A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P54205 and applied mutation signature R134A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic properties of Rubisco mutants), strain row 'R134A'; column 'Site' = Latch; column 'Kcat (min-1)' = 178; column 'Km(RuBP) (uM)' = 212; column 'apparent Km (CO2) (uM)' = 161; column 'Ki(Pi) (mM)' = 6.0. Table 2 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 178 under the column head Kcat (min-1); one min^-1 is 1/60 s^-1, so 178 / 60 = 2.966666666666667 s^(-1). km: printed Table 2 cell 212 under the column head Km(RuBP) (uM); one uM is 1/1000 mM, so 212 / 1000 = 0.212 mM. kcat/Km: Table 2 has no kcat/Km column, so nothing is converted for the ratio; the canonical catalytic efficiency is the quotient of those two converted cells of the same strain row, 2.966666666666667 / 0.212 = 13.9937106918239 s^(-1)*mM^(-1), typed derived_same_measurement against them.

raw_value_unit_evidence: Table 2, strain row R134A, site Latch: Kcat = 178 min^-1; Km(RuBP) = 212 uM. Table 2 prints no kcat/Km column, and this article prints no catalytic-efficiency cell for this measurement.

row_label: Table 2, strain row R134A, site Latch


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P54205 and applied mutation signature K305E with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic properties of Rubisco mutants), strain row 'K305E'; column 'Site' = Latch; column 'Kcat (min-1)' = 185; column 'Km(RuBP) (uM)' = 242; column 'apparent Km (CO2) (uM)' = 190; column 'Ki(Pi) (mM)' = 5.7. Table 2 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 185 under the column head Kcat (min-1); one min^-1 is 1/60 s^-1, so 185 / 60 = 3.0833333333333335 s^(-1). km: printed Table 2 cell 242 under the column head Km(RuBP) (uM); one uM is 1/1000 mM, so 242 / 1000 = 0.242 mM. kcat/Km: Table 2 has no kcat/Km column, so nothing is converted for the ratio; the canonical catalytic efficiency is the quotient of those two converted cells of the same strain row, 3.0833333333333335 / 0.242 = 12.741046831955924 s^(-1)*mM^(-1), typed derived_same_measurement against them.

raw_value_unit_evidence: Table 2, strain row K305E, site Latch: Kcat = 185 min^-1; Km(RuBP) = 242 uM. Table 2 prints no kcat/Km column, and this article prints no catalytic-efficiency cell for this measurement.

row_label: Table 2, strain row K305E, site Latch


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P54205 and applied mutation signature H310D with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic properties of Rubisco mutants), strain row 'H310D'; column 'Site' = Latch; column 'Kcat (min-1)' = 185; column 'Km(RuBP) (uM)' = 387; column 'apparent Km (CO2) (uM)' = NM; column 'Ki(Pi) (mM)' = NM. Table 2 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 185 under the column head Kcat (min-1); one min^-1 is 1/60 s^-1, so 185 / 60 = 3.0833333333333335 s^(-1). km: printed Table 2 cell 387 under the column head Km(RuBP) (uM); one uM is 1/1000 mM, so 387 / 1000 = 0.387 mM. kcat/Km: Table 2 has no kcat/Km column, so nothing is converted for the ratio; the canonical catalytic efficiency is the quotient of those two converted cells of the same strain row, 3.0833333333333335 / 0.387 = 7.967269595176572 s^(-1)*mM^(-1), typed derived_same_measurement against them.

raw_value_unit_evidence: Table 2, strain row H310D, site Latch: Kcat = 185 min^-1; Km(RuBP) = 387 uM. Table 2 prints no kcat/Km column, and this article prints no catalytic-efficiency cell for this measurement.

row_label: Table 2, strain row H310D, site Latch


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H310A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


proof_lines: wild type enzyme, in 50 mM HEPES, pH 8.0, at 30°C

proof_lines: pH 8.0, 30°C, wild-type, oxidized, mutant C172A, reduced


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R134A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K305E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


organism: Thermosynechococcus vestitus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DIS5 and applied mutation signature F345I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.1; 298.15 K; buffer reaction

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-F345I' with RbcL/RbcS mutation columns as printed in Table 1, row Te-F345I, RbcL F345I, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 14.6 +/- 0.7**; column 'kcat c (s-1)' = 4.8 +/- 0.3**; column 'Kc 21% O2 (uM)' = 101 +/- 1; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 47 +/- 2**; column 'SC/O (mol mol-1)' = 48.0 +/- 0.5**; column 'Tm (C)' = 72.3 +/- 0.3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.8 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 4.8 s^(-1); the exported value is 4.8 s^(-1). Km: printed Table 1 cell 101 uM; uM to mM is a division by 1000, so 101 / 1000 = 0.101 mM; the exported value is 0.101 mM. kcat/Km: printed Table 1 cell 47 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 47.0 s^(-1)*mM^(-1); the exported value 47.52475247524752 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-F345I, RbcL F345I, RbcS None: kcat c = 4.8 s-1; Kc 21% O2 = 101 uM; printed kcat c/Kc21%O2 = 47 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DIS5 and applied mutation signature F345I/P415A to reconstruct the assayed variant sequence.

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-FIPA' with RbcL/RbcS mutation columns as printed in Table 1, row Te-FIPA, RbcL F345I, P415A, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 17.5 +/- 1.2*; column 'kcat c (s-1)' = 4.8 +/- 0.4**; column 'Kc 21% O2 (uM)' = 102 +/- 5; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 47 +/- 6**; column 'SC/O (mol mol-1)' = 49.2 +/- 0.4**; column 'Tm (C)' = 75.9 +/- 0.1**.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.8 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 4.8 s^(-1); the exported value is 4.8 s^(-1). Km: printed Table 1 cell 102 uM; uM to mM is a division by 1000, so 102 / 1000 = 0.102 mM; the exported value is 0.102 mM. kcat/Km: printed Table 1 cell 47 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 47.0 s^(-1)*mM^(-1); the exported value 47.05882352941177 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-FIPA, RbcL F345I, P415A, RbcS None: kcat c = 4.8 s-1; Kc 21% O2 = 102 uM; printed kcat c/Kc21%O2 = 47 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DIS5 and applied mutation signature A398T/P415A to reconstruct the assayed variant sequence.

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-2Gj (15)' with RbcL/RbcS mutation columns as printed in Table 1, row Te-2Gj (15), RbcL A398T, P415A, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 16.6 +/- 3.6**; column 'kcat c (s-1)' = 6.4 +/- 0.2**; column 'Kc 21% O2 (uM)' = 110 +/- 4; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 59 +/- 3*; column 'SC/O (mol mol-1)' = 50.5 +/- 0.5**; column 'Tm (C)' = NM.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.4 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 6.4 s^(-1); the exported value is 6.4 s^(-1). Km: printed Table 1 cell 110 uM; uM to mM is a division by 1000, so 110 / 1000 = 0.11 mM; this record carries the printed cell 0.11 mM in place of the exported 0.1 mM. kcat/Km: printed Table 1 cell 59 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 59.0 s^(-1)*mM^(-1); the exported value 64.0 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-2Gj (15), RbcL A398T, P415A, RbcS None: kcat c = 6.4 s-1; Kc 21% O2 = 110 uM; printed kcat c/Kc21%O2 = 59 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DIS5 and applied mutation signature V300A to reconstruct the assayed variant sequence.

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-V300A' with RbcL/RbcS mutation columns as printed in Table 1, row Te-V300A, RbcL V300A, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 7.1 +/- 0.2; column 'kcat c (s-1)' = 6.6 +/- 0.2*; column 'Kc 21% O2 (uM)' = 135 +/- 9**; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 49 +/- 6**; column 'SC/O (mol mol-1)' = 51.9 +/- 0.6; column 'Tm (C)' = 71.4 +/- 0.6.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.6 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 6.6 s^(-1); the exported value is 6.6 s^(-1). Km: printed Table 1 cell 135 uM; uM to mM is a division by 1000, so 135 / 1000 = 0.135 mM; the exported value is 0.135 mM. kcat/Km: printed Table 1 cell 49 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 49.0 s^(-1)*mM^(-1); the exported value 48.888888888888886 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-V300A, RbcL V300A, RbcS None: kcat c = 6.6 s-1; Kc 21% O2 = 135 uM; printed kcat c/Kc21%O2 = 49 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DIS5 and applied mutation signature P415A to reconstruct the assayed variant sequence.

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-P415A' with RbcL/RbcS mutation columns as printed in Table 1, row Te-P415A, RbcL P415A, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 10.4 +/- 0.8**; column 'kcat c (s-1)' = 6.9 +/- 0.2*; column 'Kc 21% O2 (uM)' = 111 +/- 2; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 62 +/- 2*; column 'SC/O (mol mol-1)' = 52.6 +/- 0.5; column 'Tm (C)' = 73.7 +/- 0.1**.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.9 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 6.9 s^(-1); the exported value is 6.9 s^(-1). Km: printed Table 1 cell 111 uM; uM to mM is a division by 1000, so 111 / 1000 = 0.111 mM; the exported value is 0.111 mM. kcat/Km: printed Table 1 cell 62 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 62.0 s^(-1)*mM^(-1); the exported value 62.16216216216216 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-P415A, RbcL P415A, RbcS None: kcat c = 6.9 s-1; Kc 21% O2 = 111 uM; printed kcat c/Kc21%O2 = 62 mM-1 s-1.


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

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-LS (WT)' with RbcL/RbcS mutation columns as printed in Table 1, row Te-LS (WT), RbcL None, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 6.6 +/- 0.7; column 'kcat c (s-1)' = 7.4 +/- 0.1; column 'Kc 21% O2 (uM)' = 107 +/- 2; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 70 +/- 2; column 'SC/O (mol mol-1)' = 53.3 +/- 0.5; column 'Tm (C)' = 72.8 +/- 0.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 7.4 s^(-1); the exported value is 7.4 s^(-1). Km: printed Table 1 cell 107 uM; uM to mM is a division by 1000, so 107 / 1000 = 0.107 mM; the exported value is 0.107 mM. kcat/Km: printed Table 1 cell 70 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 70.0 s^(-1)*mM^(-1); the exported value 69.1588785046729 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-LS (WT), RbcL None, RbcS None: kcat c = 7.4 s-1; Kc 21% O2 = 107 uM; printed kcat c/Kc21%O2 = 70 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DIS5 and applied mutation signature I393M/P415A to reconstruct the assayed variant sequence.

column_label: Table 1: E. coli L8S8 Rubisco content and catalytic parameters at 25 C (J. Biol. Chem. 2018, 293(1):18-27), Rubisco row 'Te-2Gi (13)' with RbcL/RbcS mutation columns as printed in Table 1, row Te-2Gi (13), RbcL I393M, P415A, RbcS None; column 'Expression (% (w/w) sol E. coli protein)' = 16.6 +/- 2.4**; column 'kcat c (s-1)' = 7.8 +/- 0.4; column 'Kc 21% O2 (uM)' = 90 +/- 2**; column 'kcat c/Kc21%O2 (mM-1 s-1)' = 87 +/- 1**; column 'SC/O (mol mol-1)' = 48.1 +/- 0.4**; column 'Tm (C)' = NM.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.8 s-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 7.8 s^(-1); the exported value is 7.8 s^(-1). Km: printed Table 1 cell 90 uM; uM to mM is a division by 1000, so 90 / 1000 = 0.09 mM; the exported value is 0.09 mM. kcat/Km: printed Table 1 cell 87 mM-1 s-1; the cell is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 87.0 s^(-1)*mM^(-1); the exported value 86.66666666666667 s^(-1)*mM^(-1) is the quotient of the exported kcat and km, and this record adopts the paper's own printed efficiency cell.

raw_value_unit_evidence: Table 1, row Te-2Gi (13), RbcL I393M, P415A, RbcS None: kcat c = 7.8 s-1; Kc 21% O2 = 90 uM; printed kcat c/Kc21%O2 = 87 mM-1 s-1.


sequence_variant_note: Mutation signature P415A/Y36N/R51H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutation P415A in subunit RbcL, plus mutation Y36N/R51H in subunit RbcS, pH 8.1, 25°C