Amylase

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Alpha-amylase
Salivary alpha-amylase 1SMD.png
Human salivar amylase: calcium ion veesible in pale khaki, chloride ion in green. PDB 1SMD[1]
Identifiers
EC nummer3.2.1.1
CAS nummer9000-90-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structursRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Beta-amylase
2xfr b amylase.png
Structur o baurley beta-amylase. PDB 2xfr[2]
Identifiers
EC nummer3.2.1.2
CAS nummer9000-91-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structursRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Gamma-amylase. Glucan 1,4-alpha-glucosidase
Identifiers
EC nummer3.2.1.3
CAS nummer9032-08-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structursRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Amylase is an enzyme that catalyses the hydrolysis o stairch (Laitin amylum) intae succars.

References[eedit | eedit soorce]

  1. Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ (May 1996). "Structure of human salivary alpha-amylase at 1.6 Å resolution: implications for its role in the oral cavity". Acta Crystallographica D. 52 (3): 435–446. doi:10.1107/S0907444995014119. PMID 15299664.
  2. Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA (March 2011). "Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase". Molecular BioSystems. 7 (3): 718–730. doi:10.1039/c0mb00204f. PMID 21085740.