Post on 27-Apr-2015
ENZIMAS: HISTORIA
• Spallanzani 1783• Kühne 1836 1878• Swann 1836• Berzelius 1835• Pasteur 1850• Buchner 1897• Fischer 1894• Michaellis 1900• Sumner 1926• Northrop 1935
Ribonucleasa A pancreática bovina secuenciada 1963
Lisozima 1965 primera estructura de rayos X
Diferencias con reacciones catalizadas químicamenteAlta vel. De reacción 106-1012 más que no catalizadasCondiciones moderadas. Temp, pH, p atm.EspecificidadCapacidad de regulación
Ribozima
ENZIMAS: COMPOSICIÓN
ENZIMAS: COMPOSICIÓN
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/
NOMENCLATURA ENZIMATICA
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 50EC 4 separate up to 50EC 5 separate up to 50EC 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 dehydrogenaseEC 1.1.1.2 alcohol dehydrogenase (NADP+)
EC 1.1.1.3 homoserine dehydrogenaseEC 1.1.1.4 (R,R)-butanediol dehydrogenaseEC 1.1.1.5 acetoin dehydrogenaseEC 1.1.1.6 glycerol dehydrogenaseEC 1.1.1.7 propanediol-phosphate dehydrogenaseEC 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 acceptorEC 1.1.2.1 now EC 1.1.99.5EC 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 1.1.3.15EC 1.1.3.2 now EC 1.13.12.4EC 1.1.3.3 malate oxidaseEC 1.1.3.4 glucose oxidaseEC 1.1.3.5 hexose oxidaseEC 1.1.3.6 cholesterol oxidaseEC 1.1.3.7 aryl-alcohol oxidaseEC 1.1.3.8 L-gulonolactone oxidase
EC 1.1.4
With a disulfide as acceptorEC 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 acceptorsEC 1.1.99.1 choline dehydrogenaseEC 1.1.99.2 2-hydroxyglutarate dehydrogenaseEC 1.1.99.3 gluconate 2-dehydrogenase (acceptor)EC 1.1.99.4 dehydrogluconate dehydrogenaseEC 1.1.99.5 glycerol-3-phosphate dehydrogenaseEC 1.1.99.6 D-2-hydroxy-acid dehydrogenase
EC 1.1.99.7 lactate—malate transhydrogenaseEC 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 4.4.1.22EC 1.2.1.2 formate dehydrogenaseEC 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 acceptorEC 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 oxidaseEC 1.2.3.2 now EC 1.1.3.22EC 1.2.3.3 pyruvate oxidaseEC 1.2.3.4 oxalate oxidaseEC 1.2.3.5 glyoxylate oxidaseEC 1.2.3.6 pyruvate oxidase (CoA-acetylating)EC 1.2.3.7 indole-3-acetaldehyde oxidaseEC 1.2.3.8 pyridoxal oxidaseEC 1.2.3.9 aryl-aldehyde oxidaseEC 1.2.3.10 deletedEC 1.2.3.11 retinal oxidase
EC 1.2.4
With a disulfide as acceptorEC 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 1.2.4.4EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)
EC 1.2.7
With an iron-sulfur protein as acceptorEC 1.2.7.1 pyruvate synthaseEC 1.2.7.2 2-oxobutyrate synthaseEC 1.2.7.3 2-oxoglutarate synthaseEC 1.2.7.4 carbon-monoxide dehydrogenase (ferredoxin)
EC 1.2.99
With other acceptorsEC 1.2.99.1 now EC 1.1.99.19EC 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-reductaseEC 1.3.1.4 cortisone -reductaseEC 1.3.1.5 cucurbitacin 23-reductase
EC 1.3.1.6 fumarate reductase (NADH)
EC 1.3.2
With a cytochrome as acceptorEC 1.3.2.1 now EC 1.3.99.2EC 1.3.2.2 now EC 1.3.99.3EC 1.3.2.3 galactonolactone dehydrogenase
EC 1.3.3
With oxygen as acceptorEC 1.3.3.1 dihydroorotate oxidaseEC 1.3.3.2 now EC 1.14.21.6EC 1.3.3.3 coproporphyrinogen oxidaseEC 1.3.3.4 protoporphyrinogen oxidaseEC 1.3.3.5 bilirubin oxidaseEC 1.3.3.6 acyl-CoA oxidase
EC 1.3.5
With a quinone or related compound as acceptorEC 1.3.5.1 succinate dehydrogenase (ubiquinone)EC 1.3.7 With an iron-sulfur protein as acceptorEC 1.3.7.1 6-hydroxynicotinate reductase EC 1.3.7.2 15,16-dihydrobiliverdin:ferredoxin oxidoreductaseEC 1.3.7.3 phycoerythrobilin:ferredoxin oxidoreductaseEC 1.3.7.4 phytochromobilin:ferredoxin oxidoreductase
EC 1.3.99
With other acceptors EC 1.3.99.1 succinate dehydrogenaseEC 1.3.99.2 butyryl-CoA dehydrogenaseEC 1.3.99.3 acyl-CoA dehydrogenaseEC 1.3.99.4 3-oxosteroid 1-dehydrogenaseEC 1.3.99.5 3-oxo-5-steroid 4-dehydrogenaseEC 1.3.99.6 3-oxo-5-steroid 4-dehydrogenaseEC 1.3.99.7 glutaryl-CoA dehydrogenaseEC 1.3.99.8 2-furoyl-CoA dehydrogenaseEC 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
RETROINHIBICIÓNFeed-back
Cinética de enzimas alostericas
Enzimas reguladoras: Modificadas covalentemente
Glucógeno fosforilasa
GLUCÓGENO FOSFORILASA
Modificación covalente reversible