Centro activoCentro activo

La amilasa pancreática es una endoglicosidasa que hidroliza enlaces alfa 1-4 de poliglícidos de glucosa

para entender porqué solamente ataca los enlaces interiores del poliglícido es necesario ver cómo se coloca el poliglícido al unirse al centro activo . 1cpu muestra la estructura de la amilasa pancreática . El se muestra ocupado por 5 unidades glicídicas que son abrazadas por la hendidura del centro activo . En rojo se muestran los dos aminoácidos principales que participan en la catálisis, aspártico 197 y glutámico 233. En esta nueva visión vemos Vemos como los dos aminoácidos ácidos caen en el centro del glícido y atacan la parte central. Por tanto dado el "diseño" de este centro activo es imposible que pueda hidrolizar diglícidos con eficiencia

RegulationRegulation

α-Amylase is regulated through a number of inhibitors. These inhibitors are classified according to six categories, based on their tertiary structures^[1]. Inhibitors of α-amylase block the active site of the enzyme. In animals, inhibitors control the conversion of starch to simple sugars during glucose peaks after a meal so that breakdown of glucose occurs at a rate the body can handle^[1]. This is particularly important for diabetics, who require low quantities of α-amylase to maintain control over glucose levels. After taking insulin however, pancreatic α-amylase escalates. Plants use these inhibitors as a defense mechanism to inhibit the use of α-amylase in insects, thus protecting themselves from herbivory^[2].

3D structures of amylase (Updated on 31-October-2014)3D structures of amylase (Updated on 31-October-2014)

α-amylase
- 3ij7, 1xv8, 1c8q, 1bsi, 1smd, 1hny – hAAM – human
- 1xgz, 1q4n, 1kb3, 1kbb, 1kbk, 1kgu, 1kgw, 1kgx, 1jxj, 1jxk, 2cpu - hAAM (mutant)
- 3n8t – TkAAM – Thermococcus kodakarensis
- 3k8k – BtAAM – Bacterioides thetaiotaomicron
- 3kwx, 2guy – AoAAM – Aspergilluys oryzae
- 2wpg – AAM – Xanthomonas campestris
- 2wc7, 2wcs, 2wkg – AAM catalytic region – Cyanobacterium
- 3bh4 – BaAAM – Bacillus amyloliquefaciens
- 1e3x, 1e43 – BaAAM chimera
- 1ht6, 1amy - bAAM – barley
- 3bsg – bAAM (mutant)
- 3dhu – AAM – Lactobacillus plantarum
- 3dc0 – AAM – Bacillus KR8104
- 3bcf, 1wza – HoAAM – Halothermothrix orenii
- 2die, 1wp6 – AAM alkaline – Bacillus sp.
- 1ud2, 1ud4, 1ud5, 1ud6, 1ud8 - AAM – Bacillus sp. KSM-K38
- 1ud3 – AAM (mutant) – Bacillus sp. KSM-K38
- 2gjr – BhAAM – Bacillus halmapalus
- 2b5d – AAM – Thermotoga maritima
- 2c3g, 2c3v – BhaloAAM – Bacillus halodurans
- 1ji1, 1ji2, 1bvz - TvAAM – Thermoactinomyces vulgaris
- 1wzk, 1wzl, 1wzm, 1izj, 1izk, 1jf5, 1jf6 – TvAAM (mutant)
- 1mwo, 1mxd – PwAAM – Pyrococcus woesei
- 1ob0, 1bli - BlAAM (mutant) – Bacillus licheniformis
- 1vjs – BlAAM precursor
- 1bpl – BlAAM
- 1b0i, 1aqm, 1aqh – PhAAM - Pseudoalteromonas haloplanktis
- 1jd7, 1jd9 - PhAAM (mutant)
- 1g5a – NpAAM – Neisseria polysaccharea
- 1hvx - BaAAM – Bacillus stearothermophilus
- 1qho – GsAAM – Geobacillus stearothermophilus
- 1jae – TmAAM – Tenebrio molitor
- 1pif – pAAM – pig
- 6taa, 2aaa - AoAAM
- 4aee – AAM catalytic domain – Staphylothermus marinus
- 3ren – AAM – Clostridium perfringens
- 3vm5 – AAM – Oryzias latipes
- 3vm7 – AAM – Malbranchea cinnamomea
- 4gkl – AAM – Thermotoga neapolitana
- 4ays – AAM – Deinococcus radiodurans
- AAM binary complexes
  - 1xd0, 1xd1, 1cpu, 1jfh - hAAM + saccharide
  - 1b2y, 1xcw, 1xcx - hAAM + acarbose
  - 3blk, 3blp, 1z32, 1nm9, 1mfu, 1mfv, 3cpu - hAAM (mutant) + saccharide
  - 3dhp, 1xh0, 1xh2 - hAAM (mutant) + acarbose
  - 3ij8, 3ij9 – hAAM catalytic intermediate
  - 2qmk, 3bai – hAAM + NO2
  - 3baw – hAAM + N3
  - 3bax - hAAM (mutant) + N3
  - 3bak – hAAM (mutant) + NO3
  - 1xh1 - hAAM (mutant) + Cl
  - 2qv4, 3baj, 3bay - hAAM + acarbose + NO2
  - 3old, 3ole, 3olg, 3oli – hAAM + statin
  - 1u2y, 1u30, 1u33 – hAAM + inhibitor
  - 4gqq – hAAM + ethyl caffeate
  - 4gqr – hAAM + myricetin
  - 3n92, 3n98 – TkAAM + saccharide
  - 3l2l, 3l2m, 1vah, 1wo2, 1ua3, 1pig, 1ppi - pAAM + saccharide
  - 1hx0 – pAAM + acarbose
  - 1kxq, 1kxt, 1kxv – pAAM + antibody VHH fragment
  - 1bvn, 1dhk – pAAM + protein inhibitor
  - 1ose – pAAM + acarbose
  - 3k8l - BtAAM (mutant) + saccharide
  - 3k8m - BtAAM + acarbose
  - 2d2o, 1jl8, 1jib - TvAAM + saccharide
  - 3a6o – TvAAM + acarbose
  - 2d0f, 2d0g, 2d0h, 1vb9, 1vfm, 1vfo, 1vfu, 1uh2, 1uh4 - TvAAM (mutant) + saccharide
  - 1uh3 - TvAAM (mutant) + acarbose
  - 1ava – bAAM + protein inhibitor
  - 1bg9, 1rpk - bAAM + acarbose
  - 1p6w – bAAM + substrate analog
  - 1rp8, 1b1y, 1rp9 - bAAM (mutant) + saccharide
  - 3bsh, 2qpu, 2qps - bAAM (mutant) + acarbose
  - 3bcd - HoAAM + saccharide
  - 3bc9 - HoAAM + acarbose
  - 2gjp, 1w9x - BhAAM + saccharide
  - 2gvy - AoAAM + saccharide
  - 1zs2, 1s46, 1mvy, 1mw0, 1mw1, 1mw2, 1mw3 - NpAAM (mutant) + saccharide
  - 1bag - BsAAM + saccharide – Bacillus subtilis
  - 1ua7 – BsAAM + acarbose
  - 2d3l, 2d3n - BacAAM + saccharide – Bacillus
  - 2c3h, 2c3w, 2c3x - BhaloAAM + saccharide
  - 1mxg - PwAAM + acarbose
  - 3qgv - PwAAM + sucrose
  - 1g9h, 1g94 - PhAAM + saccharide
  - 1kxh - PhAAM (mutant) + acarbose
  - 1l0p – PhAAM + NO3
  - 1e40 – BaAAM chimera + saccharide
  - 1e3z - BaAAM chimera + acarbose
  - 1fa2 - AAM + saccharide – Sweet potato
  - 1qhp - GsAAM + saccharide
  - 4e2o - GsAAM + acarbose
  - 1clv, 1viw, 1tmq – TmAAM + protein inhibitor
  - 1gah, 1gai – AaAAM + acarbose – Aspergillus awamori
  - 3gly, 1agm, 1glm – AaAAM + saccharide
Pullulanase α-amylase
- 2wan – AAM – Bacillus acidopullululyticus
- 2fgz – KaAAM – Klebsiella aerogenes
- 2e8y - BsAAM
- 1ji2 - TvAAM
- 1jl5, 1jf6, 1wzk, 1wzl, 1wzm - TvAAM (mutant)
- Pullulanase α-amylase binary complexes
  - 2fh6, 2fh8, 2fhb, 2fhc, 2fhf - KaAAM + saccharide
  - 3fax - AAM + saccharide – Streptococcus agalactiae
  - 2e8z, 2e9b - BsAAM + saccharide
  - 2d2o - TvAAM + saccharide
  - 1g1y, 1jib, 1jl8, 1vfm, 1vfo, 1vfu, 1vb9 - TvAAM (mutant) + saccharide
  - 3a6o – TvAAM + acarbose
Neopullulanase α-amylase
- 4aef – AAM – Pyrococcus furiosus
- 1j0h – BsAAM
- 2z1k – AAM – Thermus thermophilus
- 1j0i – BsAAM + α-D-glucose
- 1j0k – BsAAM (mutant) + α-D-glucose
- 1j0j – BsAAM (mutant) + maltotetraose
β-amylase
- 2xfr – bBAM
- 1wdp – sBAM – soybean
- 2dqx, 1uko, 1ukp – sBAM (mutant)
- 1vem, 5bca, 1cqy, 1b90 – BcBAM – Bacillus cereus
- 1ven - BcBAM (mutant)
- 1fa2 - AAM + saccharide – Sweet potato
- β-amylase binary complexes
  - 2xff – bBAM + acarbose
  - 2xfy, 2xg9, 2xgb, 2xgi – bBAM + inhibitor
  - 1wdq, 1wdr, 1wds, 1v3h, 1v3i, 1q6d, 1q6e, 1q6f, 1q6g - sBAM (mutant) + saccharide
  - 1q6c, 1bfn, 1bya, 1byb, 1byc, 1byd, 1btc - sBAM + saccharide
  - 1j0y, 1j0z, 1j10, 1j11, 1j12, 1j18, 1b9z - BcBAM + saccharide
  - 1veo, 1vep, 1itc - BcBAM (mutant) + saccharide
  - 1b1y - AAM (mutant) + saccharide – Hordeum vulgare
γ-amylase
- 1lf6 – TtGAM – Thermoanaerobacterium thermosaccharolyticum
- 1lf9 - TtGAM + acarbose
β/α-amylase
- 2laa, 2lab – PpBAAM – Paenibacillus polymyxa - NMR
- 3voc – PpBAAM
Maltohexaose-producing amylase
- 1wp6 - BacMAM
- 1wpc – BacMAM + saccharide
Maltogenic amylase
- 1gvi, 1sma – MAM – Thermus sp.
Taka amylase
- 2taa, 3vx0, 3vx1 – AoTAM
- 7taa – AoTAM + acarbose

ReferencesReferences

↑ ^1.0 ^1.1 PPMID: 17713601
↑ Franco OL, Rigden DJ, Melo FR, Grossi-De-Sa MF. Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases. Eur J Biochem. 2002 Jan;269(2):397-412. PMID:11856298

[inhibit-1] 1.0 ^1.1 PPMID: 17713601

[2] Franco OL, Rigden DJ, Melo FR, Grossi-De-Sa MF. Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases. Eur J Biochem. 2002 Jan;269(2):397-412. PMID:11856298

[1]

[2]

User:Gabriel Pons/Sandbox 2

Contents

Centro activoCentro activo

RegulationRegulation

3D structures of amylase (Updated on 31-October-2014)3D structures of amylase (Updated on 31-October-2014)

ReferencesReferences