User:Gabriel Pons/Sandbox 2: Difference between revisions

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=~~Introduction~~=

=Centro activo=

Discovered and isolated by [http://en.wikipedia.org/wiki/Anselme_Payen Anselme Payen] in 1833, amylase was the first enzyme to be discovered<ref name="book">Yamamoto T.1988. Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Osaka Japan: Pergamon Press</ref>. Amylases are hydrolases, acting on α-1,4-glycosidic bonds<ref name="Path">PMID:9541387</ref>. They can be further subdivided into α,β and γ amylases<ref name="book"/>.'''α-Amylase''' (AAM) is an enzyme that acts as a catalyst for the hydrolysis of alpha-linked polysaccharides into α-anomeric products<ref name="Main">PMID:11226887</ref>. The enzyme can be derived from a variety of sources, each with different characteristics. α-Amylase found within the human body serves as the enzyme active in pancreatic juice and salvia<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries. Beta/alpha amylase (BAAM) is a precursor protein which is cleaved to form the beta-amylase and alpha-amylase after secretion.

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

~~=Structure<ref name="Main"/>=~~

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 <scene name='42/428167/Centro_activo/1'>centro activo </scene>se muestra ocupado por 5 unidades glicídicas que son abrazadas por la hendidura del centro activo .The <scene name='Sandbox_182/Domain_a/1'> B domain</scene> consists of a sheet of four anti-parallel β-strands with a pair of anti-parallel β-strands. Long loops are observed between the β-strands. Located within the B domain is the <scene name='Sandbox_182/Trio/1'>binding site</scene> for Ca2+-Na+-Ca2+. <scene name='Sandbox_182/Domain_c/1'>Domain C </scene>consisting of eight β-strands is assembled into a globular unit forming a Greek key motif. It also holds the <scene name='Sandbox_182/Caiii/1'>third </scene>Ca2+ binding site in association with domain A. Positioned on the C-terminal side of the β-strands of the (β/α)8-barrel in domain A is the active site. The catalytic residues involved for the BSTA active site are

~~Shown as 1hvx is the structure of the thermostable α-amylase of ''Bacillus stearothermophilus'' (BSTA)<ref name="Main"/>. BSTA is comprised of a single polypeptide chain~~. ~~This chain is folded into three domains: A, B and C~~. ~~These domains are generally found on all α-amylase enzymes. The~~ <scene name='~~Sandbox_182~~/~~Domain_aa~~/1'>~~A domain~~ </scene>~~constitutes the core structure, with a (β/α)8-barrel~~.The <scene name='Sandbox_182/Domain_a/1'> B domain</scene> consists of a sheet of four anti-parallel β-strands with a pair of anti-parallel β-strands. Long loops are observed between the β-strands. Located within the B domain is the <scene name='Sandbox_182/Trio/1'>binding site</scene> for Ca2+-Na+-Ca2+. <scene name='Sandbox_182/Domain_c/1'>Domain C </scene>consisting of eight β-strands is assembled into a globular unit forming a Greek key motif. It also holds the <scene name='Sandbox_182/Caiii/1'>third </scene>Ca2+ binding site in association with domain A. Positioned on the C-terminal side of the β-strands of the (β/α)8-barrel in domain A is the active site. The catalytic residues involved for the BSTA active site are

<scene name='Sandbox_182/Active_site/1'>Asp234, Glu264, and Asp331</scene>. The residues are identical to other α-amylases, yet there are positional differences which reflect the flexible nature of catalytic resides.

<scene name='Sandbox_182/Trio/1'>CaII and CaI with Na</scene> found in the interior of domain B and <scene name='Sandbox_182/Caiii/2'>CaIII </scene>at the interface of domain A and C, constitute the metal ion binding sites. All α-amylases contain one strongly conserved Ca2+ ion for structural integrity and enzymatic activity.<ref name="chloride">PMID: 12021442</ref> CaI is consistent in α-amylases, however there are structural differences between the linear trio of CaI, CaII and Na in other enzymes. CaIII acts as a bridge between two loops, one from α6 of domain A, and one between β1 and β2 of domain C.

@@ Line 1: / Line 1: @@
-<StructureSection load='1cpu' size='400' side='right' scene='42/428167/Vision_general/1' caption='Amilasa con los aminoácidos del centro activo (rojo) (PDB code [[1cpu]])'>
+<StructureSection load='1cpu' size='400' side='right' scene='42/428167/Vision_general/1' caption='Amilasa con los aminoácidos del centro activo (rojo) (PDB code 1cpu)'>
-=Introduction=
+=Centro activo=
-Discovered and isolated by [http://en.wikipedia.org/wiki/Anselme_Payen Anselme Payen] in 1833, amylase was the first enzyme to be discovered<ref name="book">Yamamoto T.1988. Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Osaka Japan: Pergamon Press</ref>. Amylases are hydrolases, acting on α-1,4-glycosidic bonds<ref name="Path">PMID:9541387</ref>. They can be further subdivided into α,β and γ amylases<ref name="book"/>.'''α-Amylase''' (AAM) is an enzyme that acts as a catalyst for the hydrolysis of alpha-linked polysaccharides into α-anomeric products<ref name="Main">PMID:11226887</ref>. The enzyme can be derived from a variety of sources, each with different characteristics. α-Amylase found within the human body serves as the enzyme active in pancreatic juice and salvia<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries.  Beta/alpha amylase (BAAM) is a precursor protein which is cleaved to form the beta-amylase and alpha-amylase after secretion.
+La amilasa pancreática es una endoglicosidasa que hidroliza enlaces alfa 1-4 de poliglícidos de glucosa
-=Structure<ref name="Main"/>=
+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 <scene name='42/428167/Centro_activo/1'>centro activo </scene>se muestra ocupado por 5 unidades glicídicas que son abrazadas por la hendidura del centro activo .The <scene name='Sandbox_182/Domain_a/1'> B domain</scene> consists of a sheet of four anti-parallel β-strands with a pair of anti-parallel  β-strands. Long loops are observed between the β-strands.  Located within the B domain is the <scene name='Sandbox_182/Trio/1'>binding site</scene> for Ca<sup>2+</sup>-Na<sup>+</sup>-Ca<sup>2+</sup>. <scene name='Sandbox_182/Domain_c/1'>Domain C </scene>consisting of eight β-strands is assembled into a globular unit forming a Greek key motif.  It also holds the <scene name='Sandbox_182/Caiii/1'>third </scene>Ca<sup>2+</sup> binding site in association with domain A. Positioned on the C-terminal side of the β-strands of the (β/α)<sub>8</sub>-barrel in domain A is the active site.  The catalytic residues involved for the BSTA active site are
-Shown as 1hvx is the structure of the thermostable α-amylase of ''Bacillus stearothermophilus'' (BSTA)<ref name="Main"/>. BSTA is comprised of a single polypeptide chain. This chain is folded into three domains: A, B and C. These domains are generally found on all α-amylase enzymes. The <scene name='Sandbox_182/Domain_aa/1'>A domain </scene>constitutes the core structure, with a (β/α)<sub>8</sub>-barrel.The <scene name='Sandbox_182/Domain_a/1'> B domain</scene> consists of a sheet of four anti-parallel β-strands with a pair of anti-parallel  β-strands. Long loops are observed between the β-strands.  Located within the B domain is the <scene name='Sandbox_182/Trio/1'>binding site</scene> for Ca<sup>2+</sup>-Na<sup>+</sup>-Ca<sup>2+</sup>. <scene name='Sandbox_182/Domain_c/1'>Domain C </scene>consisting of eight β-strands is assembled into a globular unit forming a Greek key motif.  It also holds the <scene name='Sandbox_182/Caiii/1'>third </scene>Ca<sup>2+</sup> binding site in association with domain A. Positioned on the C-terminal side of the β-strands of the (β/α)<sub>8</sub>-barrel in domain A is the active site.  The catalytic residues involved for the BSTA active site are
 <scene name='Sandbox_182/Active_site/1'>Asp234, Glu264, and Asp331</scene>. The residues are identical to other α-amylases, yet there are positional differences which reflect the flexible nature of catalytic resides.
 <scene name='Sandbox_182/Trio/1'>CaII and CaI with Na</scene> found in the interior of domain B and <scene name='Sandbox_182/Caiii/2'>CaIII </scene>at the interface of domain A and C, constitute the metal ion binding sites. All α-amylases contain one strongly conserved Ca<sup>2+</sup> ion for structural integrity and enzymatic activity.<ref name="chloride">PMID: 12021442</ref> CaI is consistent in α-amylases, however there are structural differences between the linear trio of CaI, CaII and Na in other enzymes. CaIII acts as a bridge between two loops, one from α6 of domain A, and one between β1 and β2 of domain C.