enzim isomerase 6.pptx

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    ISOMERASE ENZYME10412002 Halida Balebi

    10412003 Rohmah Nasada Tuita

    10412013 Qonita Afinanisa

    10412016 Fadilla Zahra Putri

    10412020 Ruli Fatmawati

    10412021 Faizah Khoirunnisaa

    10412023 Ratna Eka Putri

    10412025 Nurhayati Abdullah

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    Enzyme Classification Based on

    International Union of Biochemistry and Molecular Biology

    EC 1 : Oxydoreductase

    EC 2 : Transferase

    EC 3 : Hidrolase

    EC 4 : Lyase

    EC 5 : Isomerase

    EC 6 : Ligase

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    ISOMERASESThe fifth class of enzyme that catalyze structural changes within

    a molecule. There is only one substrate and one product with

    nothing gained or lost, so they represent only a change in shape.

    Isomers have the same molecular formula but differ in their

    structural formula. These differences can change the chemical

    properties of the molecule.

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    EC (Enzyme Commission) number: scheme by numeric

    nomenclature based on catalyzed reaction, consist of 4 digit

    number

    5.x.y.z5 : isomerase enzyme

    x: subclass (based on type isomerism)

    y: sub- subclass (based on type of substrate)

    z: enzyme sequence

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    TRIVIAL NAME(SUBSTRATE) (ISOMERASE/TYPE OF ISOMERASE)

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    .

    X(subclass) Y(sub-sub class) Z(enzyme

    sequence)

    Contoh

    5.1

    Racemases

    and

    epimerases

    (racemizationand

    epimerization

    of a centre of

    chirality)

    5.1.1

    amino acids and derivatives

    5.1.1.1-

    5.1.1.18

    EC 5.1.1.3

    glutamate racemase

    5.1.2

    hydroxy acids and derivatives

    1-6 EC 5.1.2.6

    isocitrate epimerase

    5.1.3

    carbohydrates and

    derivatives

    1-23 EC 5.1.3.21

    maltose epimerase

    5.1.99

    other compounds

    1-5 EC 5.1.99.2

    16-hydroxysteroid epimerase

    5.2cis-trans-

    Isomerases

    5.2.1enzymes that rearrange the geometry

    at double bonds (cis-trans isomerases)

    5.2.1.1-5.2.1.10

    EC 5.2.1.1malat isomerase

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    X

    (subclass)

    Y

    (sub-sub class)

    Z

    (enzyme

    sequence)

    Contoh

    3

    Intramolecular

    oxidoreductase

    s

    1

    Interconverting in the sugar series,

    aldoses and ketoses, and related

    compounds (sugar isomerases)

    1-28 EC 5.3.1.5

    D-xylose aldose-ketose isomerase

    2

    catalysing a keto-enol equilibrium

    1-2 EC 5.3.2.1

    Phenylpyruvate keto-enol isomerase

    3

    enzymes shifting a carbon-carbon

    double bond from one

    position to another

    1-15 EC 5.3.3.8

    dodecenoyl-CoA isomerase

    4

    enzymes transposing S-S bonds

    1 EC 5.3.4.1

    protein disulfide-isomerase

    99

    a group of miscellaneous enzymes

    1-9 EC 5.3.99.9

    neoxanthin synthase

    4

    Intramoleculartransferases

    1

    acyl group

    1-2 EC 5.4.1.1

    Lysolecithin 2,3-acylmutase

    2

    phospho group

    1-10 EC 5.4.2.1

    D-phopoglycerate 2,3 phospomutase

    3

    amino group

    1-10 EC 5.4.3.6

    tyrosine 2,3-aminomutase

    4

    hydroxy group

    1-3 EC 5.4.4.3

    3-(hydroxyamino)phenol mutase99 1-18 EC 5.4.99.11

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    X

    (subclass)

    Y

    (sub-sub class)

    Z

    (enzyme sequence)

    contoh

    5

    Intramolecuar lyase

    1

    Berdasarkan waktu

    ditemukan

    1-16 EC 5.5.1.5

    3-carboxy-2,5-

    dihydro-5-oxofuran-

    2-acetate lyase

    99

    Other isomerase

    1

    Sole subclass of

    isomerase that do

    not belong in the

    other subclasses

    1-4 EC 5.99.1.3

    DNA topoisomerase

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    EC 5.1.1.1Accepted name: alanine racemase

    IUBMB name : EC 5.1.1.1

    Reaction: L-alanine D-alanine

    Other name(s): L-alanine racemase

    Systematic name: alanine racemase

    EC 5. Isomerase

    EC 5.1 Racemases and epimerases

    EC 5.1.1. amino acids and derivatives

    EC5.1.1.1

    Alanine racemase

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    Mechanism Reaction

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    EC 5.2.1.1Accepted name: maleat isomerase

    IUBMB name : EC 5.2.1.1Reaction: maleate fumarate

    Systematic name: maleat cis-trans-isomerase

    EC 5. Isomerase

    EC 5.2 CisTrans Isomerase

    EC 5.2.1. Cistrans Isomerase

    EC5.2.1.1 Maleate Isomerase

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    Mechanism Reaction

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    Mechanism Reaction

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    EC 5.3.1.5Accepted name: Xylose Isomerase

    IUBMB name : EC 5.3.1.5

    Reaction: D-xylose D-xyluloseD-glucose D-fructose

    Other name(s): D-xylose isomerase; D-xylose ketoisomerase; D-xylose ketol-isomerase

    Systematic name: D-xylose aldose-ketose-isomerase

    EC 5. Isomerase

    EC 5.3 Intramolecularoxidoreductases

    EC 5.3.1. Interconverting aldoses and

    ketoses, and relatedcompounds

    EC5.3.1.5

    Xylose isomerase

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    Mechanism Reactions1. Isomerization proceeds via

    a hydride-shift mechanism.

    enzyme binds the closed

    form of its sugar substrate

    (in the case of glucose, only

    the alpha anomer)

    catalyzes ring opening to

    generate open-chain

    conformation that is

    coordinated to one of the

    metal sites2. Hydrogen transfer is the

    rate-determining step for the

    enzymes.

    Essential histidine

    functions to stabilize the

    transition state byhydrogen bonding to the

    C5 hydroxyl group of the

    substrate,

    enabling a metal-catalyzed

    hydride shift from C2 to C1.

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    EC 5.4.2.1

    Accepted name: phosphoglycerate mutase

    IUBMB name : EC 5.4.2.1Reaction: 2-phospho-D-glycerate 3-phospho-D-glycerate

    Systematic name: D-phosphoglycerate 2,3- phosphomutase

    EC 5. Isomerase

    EC 5.4 Intramolecular transferases

    EC 5.4.2. phospho group

    EC 5.4.2.1 MaleateIsomerase

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    Mechanism Reaction

    (a) 3-phosphoglycerate binds to the phosphoenzyme.

    (b) Transfering the phosphoryl group to the substrate forms theintermediate 2,3-bisphosphoglycerate. The enzyme must notrelease the intermediate in order to remain active.

    (c) 2-phosphoglycerate with phosphoenzyme.

    Cronk, J.D. 2012

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    EC 5.5.1.7

    Accepted name: chloromuconate cycloisomerase

    IUBMB name : EC 5.5.1.7Reaction: 2-chloro-2,5-dihydro-5-oxofuran-2-acetate 3-chloro-cis,cis-muconate

    Other name(s): muconate cycloisomerase II

    Systematic name : 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)

    EC 5. Isomerase

    EC 5.5 Intramolecular lyases

    EC 5.5.X. Intramolecular lyases (only

    sub-subclass identified todate)

    EC 5.5.1.7 Chloromuconatecycloisomerase

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    Mechanism Reaction

    Chloromuconate cycloisomerase converts 3-chloro-cis,cis-muconate to cis-

    dienelactone (cis-4-carboxymethylenebut-2-en-4-olide by either

    dehydrohalogenation of 4-chloromuconolactone or, more directly, by chlorideelimination from the enol/enolate intermediate

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    EC 5.99

    (Other isomerases)

    This subclass containsmiscellaneous enzymes in

    a single sub-subclass (EC

    5.99.1).

    Examples : thiocyanateisomerase, DNA

    topoisomerase, 2-

    hydroxychromene-2-

    carboxylate isomerase

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    References

    Chanitnun, K., Pinphanichakarn, P. 2012. Glucose(xylose) isomerase production byStreptomyces sp. CH7 grown on agricultural residues. Braz. J. Microbiol., 43(3) : 1 7

    Cronk, J.D. 2012. Phosphoglycerate Mutase.

    http://guweb2.gonzaga.edu/faculty/cronk/biochem/P-

    index.cfm?definition=phosphoglycerate_mutase. Diakses pada tanggal 16 September

    2014.

    Lee, C. Y., Bagdasarian, M., Meng, M. H., Zeikus, J. G. 1990. Catalytic mechanism of xylose(glucose) isomerase from Clostridium thermosulfurogenes. Characterization of the

    structural gene and function of active site histidine.J Biol Chem, 265 (31):19082-90

    http://chemwiki.ucdavis.edu/Organic_Chemistry/Organic_Chemistry_With_a_Biological_Em

    phasis/Chapter_14%3A_Reactions_with_stabilized_carbanion_intermediates_II/Section

    _14.4%3A_Pyridoxal_phosphate_-_an_electron_sink_cofactor

    http://www.chem.qmul.ac.uk/iubmb/enzyme/EC5/http://www.enzyme-database.org/downloads/ec5.pdf

    Setiyabudi, L. 2008. Analisis Komputasi, Isolasi, Ekspresi, Purifikasi, dan Karakterisasi

    Triosephosphate Isomerasedari Trypanosoma cruziStrain Ninoa.

    http://old.analytical.chem.itb.ac.id/coursesdata/96/moddata/forumtt/13/456/EC._5.3.1.

    1_TPI_10505090_LuluSetiyabudi.doc. Diakses 16 September 2014