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AMY2A

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Mammalian protein found in Homo sapiens

AMY2A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1B2Y, 1BSI, 1CPU, 1HNY, 1KB3, 1KBB, 1KBK, 1KGU, 1KGW, 1KGX, 1U2Y, 1U30, 1U33, 1XCW, 1XCX, 1XD0, 1XD1, 1XGZ, 1XH0, 1XH1, 1XH2, 2CPU, 2QMK, 2QV4, 3BAI, 3BAJ, 3BAK, 3BAW, 3BAX, 3BAY, 3CPU, 3IJ7, 3IJ8, 3IJ9, 3OLD, 3OLE, 3OLG, 3OLI, 4GQQ, 4GQR, 4W93, 4X9Y, 5EMY

Identifiers
AliasesAMY2A, AMY2, AMY2B, PA, amylase, alpha 2A (pancreatic), amylase alpha 2A (pancreatic), amylase alpha 2A
External IDsOMIM: 104650; MGI: 88019; HomoloGene: 20179; GeneCards: AMY2A; OMA:AMY2A - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)
Chromosome 1 (human)Genomic location for AMY2AGenomic location for AMY2A
Band1p21.1Start103,617,427 bp
End103,625,780 bp
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)
Chromosome 3 (mouse)Genomic location for AMY2AGenomic location for AMY2A
Band3 F3|3 49.35 cMStart113,349,359 bp
End113,400,348 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • islet of Langerhans

  • duodenum

  • testicle

  • nucleus accumbens

  • fundus

  • ectocervix

  • putamen

  • caudate nucleus

  • right lobe of liver
Top expressed in
  • parotid gland

  • lacrimal gland

  • submandibular gland

  • intercostal muscle

  • left lobe of liver

  • white adipose tissue

  • neural layer of retina

  • tunica adventitia of aorta

  • subcutaneous adipose tissue

  • lactiferous gland
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

279

11722

Ensembl

ENSG00000243480

ENSMUSG00000074264

UniProt

P04746

P00687

RefSeq (mRNA)

NM_000699

NM_001110505
NM_007446

RefSeq (protein)

NP_000690

NP_001103975
NP_031472

Location (UCSC)Chr 1: 103.62 – 103.63 MbChr 3: 113.35 – 113.4 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene.

Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000243480Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000074264Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR (Jul 1988). "Human pancreatic amylase is encoded by two different genes". Nucleic Acids Res. 16 (10): 4724. doi:10.1093/nar/16.10.4724. PMC 336663. PMID 3260028.
  6. ^ "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic".

External links

See also

Further reading

PDB gallery
  • 1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE 1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE
  • 1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN 1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN
  • 1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE 1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE
  • 1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT 1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
  • 1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes 1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
  • 1jxj: Role of mobile loop in the mechanism of human salivary amylase 1jxj: Role of mobile loop in the mechanism of human salivary amylase
  • 1jxk: Role of the mobile loop in the mechanism of human salivary amylase 1jxk: Role of the mobile loop in the mechanism of human salivary amylase
  • 1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase 1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase
  • 1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids 1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
  • 1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids 1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
  • 1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE 1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE
  • 1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE 1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE
  • 1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase 1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase
  • 1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant 1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant
  • 1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme 1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme
  • 1nm9: Crystal structure of recombinant human salivary amylase mutant W58A 1nm9: Crystal structure of recombinant human salivary amylase mutant W58A
  • 1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity 1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
  • 1smd: HUMAN SALIVARY AMYLASE 1smd: HUMAN SALIVARY AMYLASE
  • 1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam 1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam
  • 1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam 1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam
  • 1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors 1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors
  • 1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xgz: Structure of the N298S variant of human pancreatic alpha-amylase 1xgz: Structure of the N298S variant of human pancreatic alpha-amylase
  • 1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose 1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose
  • 1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride 1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride
  • 1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose 1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose
  • 1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer 1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer
  • 1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues 1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues
  • 2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT 2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
  • 3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT 3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT


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