Arabinanase: Difference between revisions
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<StructureSection load='1gye' size='400' side='right' caption='Endo-arabinanase complex with arabinohexose (yellow) and Cl- ion (green) (PDB code [[1gye]])' scene='45/451702/Cv/1'> | |||
''' | |||
== Function == | |||
'''Arabinanase''' (Ara) hydrolyzes the α-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans.<ref>PMID:19505290</ref> See more details in [[Exo-alpha-1,5-L-Arabinanase]]. '''Endo-arabinanase''' hydrolyzes from the N-terminal of the chain while '''exo-arabinanase''' hydrolyzes from the end of the chain. | |||
== Structural highlights == | |||
The <scene name='45/451702/Cv/4'>active site of Ara is composed of 3 acidic residues</scene>.<ref>PMID:12198486</ref>. <scene name='45/451702/Cv/5'>Whole active site</scene>. | |||
*<scene name='45/451702/Cv/7'>Arabinohexose binding pocket</scene>. | |||
*<scene name='45/451702/Cv/6'>Cl coordination site</scene>. | |||
== 3D Structures of Arabinanase == | == 3D Structures of Arabinanase == | ||
[[Arabinanase 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
Latest revision as of 12:03, 27 May 2024
FunctionArabinanase (Ara) hydrolyzes the α-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans.[1] See more details in Exo-alpha-1,5-L-Arabinanase. Endo-arabinanase hydrolyzes from the N-terminal of the chain while exo-arabinanase hydrolyzes from the end of the chain. Structural highlightsThe .[2]. .
3D Structures of Arabinanase
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ReferencesReferences
- ↑ Alhassid A, Ben-David A, Tabachnikov O, Libster D, Naveh E, Zolotnitsky G, Shoham Y, Shoham G. Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate. Biochem J. 2009 Jul 29;422(1):73-82. PMID:19505290 doi:10.1042/BJ20090180
- ↑ Nurizzo D, Turkenburg JP, Charnock SJ, Roberts SM, Dodson EJ, McKie VA, Taylor EJ, Gilbert HJ, Davies GJ. Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold. Nat Struct Biol. 2002 Sep;9(9):665-8. PMID:12198486 doi:10.1038/nsb835