ENZIMAS: HISTORIA

 L. Spallanzani 1783
 Kühne 1836 1878
 Swann 1836
 Berzelius 1835
 Pasteur 1850
 Buchner 1897 1907
 Fischer 1894
 Michaellis 1900
 Sumner 1926 1946
 Northrop 1935 1946
Ribonucleasa A pancreática bovina
secuenciada 1963

Lisozima 1965 primera estructura

de rayos X
Diferencias con reacciones catalizadas químicamente
Alta vel. De reacción 106-1012 más que no catalizadas
Condiciones moderadas. Temp, pH, p atm.
Especificidad
Capacidad de regulación
Ribozima
ENZIMAS: COMPOSICIÓN
ENZIMAS: COMPOSICIÓN
 NOMENCLATURA ENZIMATICA

Recommendations of the Nomenclature Committee of the International Union of

Biochemistry and Molecular Biology on the Nomenclature and Classification of
Enzymes by the Reactions they Catalyse
http://www.chem.qmul.ac.uk/iubmb/enzyme/
List of Recommended Names for Enzymes
The common names of all listed enzymes are listed below, along with
their EC numbers. Where an enzyme has been deleted or transferred to
another EC number, this information is also indicated. Each list is linked
to either separate entries for each entry or to files with up to 50
enzymes in each file.

Common Names for: List linked to:

EC 1.1 to EC 1.3 separate up to 50

EC 1.4 to EC 1.97 separate up to 50

EC 2.1 to EC 2.4.1 separate up to 50

EC 2.4.2 to EC 2.9 separate up to 50

EC 3.1 to EC 3.3 separate up to 50

EC 3.4 to EC 3.12 separate up to 50
EC 4 separate up to 50
EC 5 separate up to 50
EC 6 separate up to 50
EC 1 Oxidoreductases
EC 1.1 Acting on the CH-OH group of donors
EC 1.1.1 With NAD+ or NADP as acceptor
+

EC 1.1.1.1 alcohol dehydrogenase

EC 1.1.1.2 alcohol dehydrogenase (NADP+)
EC 1.1.1.3 homoserine dehydrogenase
EC 1.1.1.4 (R,R)-butanediol dehydrogenase
EC 1.1.1.5 acetoin dehydrogenase
EC 1.1.1.6 glycerol dehydrogenase
EC 1.1.1.7 propanediol-phosphate dehydrogenase
EC 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+)
EC 1.1.1.9 D-xylulose reductase
EC 1.1.1.10 L-xylulose reductase
EC 1.1.1.11 D-arabinitol 4-dehydrogenase
EC 1.1.1.12 L-arabinitol 4-dehydrogenase
EC 1.1.1.13 L-arabinitol 2-dehydrogenase
EC 1.1.2
With a cytochrome as acceptor
EC 1.1.2.1 now EC 1.1.99.5
EC 1.1.2.2 mannitol dehydrogenase (cytochrome)
EC 1.1.2.3 L-lactate dehydrogenase (cytochrome)
EC 1.1.2.4 D-lactate dehydrogenase (cytochrome)
EC 1.1.2.5 D-lactate dehydrogenase (cytochrome c-553)
EC 1.1.3 With oxygen as acceptor

EC 1.1.3.1 deleted, included in EC 1.1.3.15

EC 1.1.3.2 now EC 1.13.12.4
EC 1.1.3.3 malate oxidase
EC 1.1.3.4 glucose oxidase
EC 1.1.3.5 hexose oxidase
EC 1.1.3.6 cholesterol oxidase
EC 1.1.3.7 aryl-alcohol oxidase
EC 1.1.3.8 L-gulonolactone oxidase
EC 1.1.4
With a disulfide as acceptor
EC 1.1.4.1 vitamin-K-epoxide reductase (warfarin-sensitive)
EC 1.1.4.2 vitamin-K-epoxide reductase (warfarin-insensitive)
EC 1.1.5 With a quinone or similar compound as acceptor

EC 1.1.5.1 deleted, see EC 1.1.99.18

EC 1.1.5.2 quinoprotein glucose dehydrogenase
EC 1.1.99
With other acceptors
EC 1.1.99.1 choline dehydrogenase
EC 1.1.99.2 2-hydroxyglutarate dehydrogenase
EC 1.1.99.3 gluconate 2-dehydrogenase (acceptor)
EC 1.1.99.4 dehydrogluconate dehydrogenase
EC 1.1.99.5 glycerol-3-phosphate dehydrogenase
EC 1.1.99.6 D-2-hydroxy-acid dehydrogenase
EC 1.1.99.7 lactate—malate transhydrogenase
EC 1.1.99.8 alcohol dehydrogenase (acceptor)
EC 1.2 Acting on the aldehyde or oxo group of donors
EC 1.2.1 With NAD+ or NADP as acceptor
+

EC 1.2.1.1 deleted, replaced by EC 1.1.1.284 and EC 4.4.1.22

EC 1.2.1.2 formate dehydrogenase
EC 1.2.1.3 aldehyde dehydrogenase (NAD+)
EC 1.2.1.4 aldehyde dehydrogenase (NADP+)
EC 1.2.1.5 aldehyde dehydrogenase [NAD(P)+]
EC 1.2.1.6 deleted
EC 1.2.2
With a cytochrome as acceptor
EC 1.2.2.1 formate dehydrogenase (cytochrome)
EC 1.2.2.2 pyruvate dehydrogenase (cytochrome)
EC 1.2.2.3 formate dehydrogenase (cytochrome-c-553)
EC 1.2.2.4 carbon-monoxide dehydrogenase (cytochrome-b-561)
EC 1.2.3 With oxygen as acceptor

EC 1.2.3.1 aldehyde oxidase

EC 1.2.3.2 now EC 1.1.3.22
EC 1.2.3.3 pyruvate oxidase
EC 1.2.3.4 oxalate oxidase
EC 1.2.3.5 glyoxylate oxidase
EC 1.2.3.6 pyruvate oxidase (CoA-acetylating)
EC 1.2.3.7 indole-3-acetaldehyde oxidase
EC 1.2.3.8 pyridoxal oxidase
EC 1.2.3.9 aryl-aldehyde oxidase
EC 1.2.3.10 deleted
EC 1.2.3.11 retinal oxidase
EC 1.2.4
With a disulfide as acceptor
EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring)
EC 1.2.4.2 oxoglutarate dehydrogenase (succinyl-transferring)
EC 1.2.4.3 deleted, included in EC 1.2.4.4
EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-
methylpropanoyl-transferring)
EC 1.2.7
With an iron-sulfur protein as acceptor
EC 1.2.7.1 pyruvate synthase
EC 1.2.7.2 2-oxobutyrate synthase
EC 1.2.7.3 2-oxoglutarate synthase
EC 1.2.7.4 carbon-monoxide dehydrogenase (ferredoxin)
EC 1.2.99
With other acceptors
EC 1.2.99.1 now EC 1.1.99.19
EC 1.2.99.2 carbon-monoxide dehydrogenase (acceptor)
EC 1.2.99.3 aldehyde dehydrogenase (pyrroloquinoline-quinone)
EC 1.2.99.4 formaldehyde dismutase
EC 1.3 Acting on the CH-CH group of donors
EC 1.3.1 With NAD+ or NADP as acceptor
+

EC 1.3.1.1 dihydrouracil dehydrogenase (NAD+)

EC 1.3.1.2 dihydropyrimidine dehydrogenase (NADP+)
EC 1.3.1.3 4-3-oxosteroid 5-reductase
EC 1.3.1.4 cortisone -reductase
EC 1.3.1.5 cucurbitacin 23-reductase
EC 1.3.1.6 fumarate reductase (NADH)
EC 1.3.2
With a cytochrome as acceptor
EC 1.3.2.1 now EC 1.3.99.2
EC 1.3.2.2 now EC 1.3.99.3
EC 1.3.2.3 galactonolactone dehydrogenase
EC 1.3.3
With oxygen as acceptor
EC 1.3.3.1 dihydroorotate oxidase
EC 1.3.3.2 now EC 1.14.21.6
EC 1.3.3.3 coproporphyrinogen oxidase
EC 1.3.3.4 protoporphyrinogen oxidase
EC 1.3.3.5 bilirubin oxidase
EC 1.3.3.6 acyl-CoA oxidase
EC 1.3.5
With a quinone or related compound as acceptor
EC 1.3.5.1 succinate dehydrogenase (ubiquinone)
EC 1.3.7 With an iron-sulfur protein as acceptor
EC 1.3.7.1 6-hydroxynicotinate reductase
EC 1.3.7.2 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
EC 1.3.7.3 phycoerythrobilin:ferredoxin oxidoreductase
EC 1.3.7.4 phytochromobilin:ferredoxin oxidoreductase
EC 1.3.99
With other acceptors
EC 1.3.99.1 succinate dehydrogenase
EC 1.3.99.2 butyryl-CoA dehydrogenase
EC 1.3.99.3 acyl-CoA dehydrogenase
EC 1.3.99.4 3-oxosteroid 1-dehydrogenase
EC 1.3.99.5 3-oxo-5-steroid 4-dehydrogenase
EC 1.3.99.6 3-oxo-5-steroid 4-dehydrogenase
EC 1.3.99.7 glutaryl-CoA dehydrogenase
EC 1.3.99.8 2-furoyl-CoA dehydrogenase
EC 1.3.99.9 now EC 1.21.99.1
EC 1.1.1.1
Common name: alcohol dehydrogenase
Reaction: an alcohol + NAD+ = an aldehyde or ketone + NADH +
H+
Other name(s): aldehyde reductase; ADH; alcohol dehydrogenase
(NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase;
NAD-dependent alcohol dehydrogenase; NAD-specific aromatic
alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-
aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast
alcohol dehydrogenase
Systematic name: alcohol:NAD+ oxidoreductase
Comments: A zinc protein. Acts on primary or secondary alcohols
or hemi-acetals; the animal, but not the yeast, enzyme acts also on
cyclic secondary alcohols.
QUIMOTRIPSINA: SITIO ACTIVO
Quimotrisina. Estructura
Dihidrofolato reductasa: Efecto de la coenzima
ENERGÍA DE ACTIVACIÓN. PODER CATALÍTICO
Estado de transición. Interacciones débiles E-S
Disminución de entropía – Mayor velocidad
Aminoácidos en catálisis ácido-base
CINÉTICA ENZIMÁTICA
Kcat. Nº de Recambio
Kcat/Km. Constante de Especificidad
Cambios en el sustrato afectan actividad de Quimotripsina
Reacciones con 2 sustratos: Mecanismos
EFECTO DEL pH
ENZIMAS REGULADORAS: ALOSTERICAS
Transcarbamiolasa. Enzima alostérica
RETROINHIBICIÓN
Feed-back
Cinética de enzimas alostericas
Enzimas reguladoras: Modificadas covalentemente

Glucógeno fosforilasa
GLUCÓGENO FOSFORILASA
Modificación covalente reversible