Sequence of AMY1_HORVU
EC Number:3.2.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose
Other sequences found for EC No. 3.2.1.1
General information:
Sequence
0 MGKNGSLCCF SLLLLLLLAG LASGHQVLFQ GFNWESWKQS GGWYNMMMGK VDDIAAAGVT
60 HVWLPPPSHS VSNEGYMPGR LYDIDASKYG NAAELKSLIG ALHGKGVQAI ADIVINHRCA
120 DYKDSRGIYC IFEGGTSDGR LDWGPHMICR DDTKYSDGTA NLDTGADFAA APDIDHLNDR
180 VQRELKEWLL WLKSDLGFDA WRLDFARGYS PEMAKVYIDG TSPSLAVAEV WDNMATGGDG
240 KPNYDQDAHR QNLVNWVDKV GGAASAGMVF DFTTKGILNA AVEGELWRLI DPQGKAPGVM
300 GWWPAKAATF VDNHDTGSTQ AMWPFPSDKV MQGYAYILTH PGIPCIFYDH FFNWGFKDQI
360 AALVAIRKRN GITATSALKI LMHEGDAYVA EIDGKVVVKI GSRYDVGAVI PAGFVTSAHG
420 NDYAVWEKNG AAATLQRS
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
4334
Rogers J.C.,Milliman C.
Isolation and sequence analysis of a barley alpha-amylase cDNA clone.
J. Biol. Chem.
258
8169-8174
1983
4335
Sogaard M.,Kadziola A.,Haser R.,Svensson B.
Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1.
J. Biol. Chem.
268
22480-22484
1993
4336
Nielsen M.M.,Bozonnet S.,Seo E.S.,Motyan J.A.,Andersen J.M.,Dilokpimol A.,Abou Hachem M.,Gyemant G.,Naested H.,Kandra L.,Sigurskjold B.W.,Svensson B.
Two secondary carbohydrate binding sites on the surface of barley alpha-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules.
Biochemistry
48
7686-7697
2009
4337
Seung D.,Thalmann M.,Sparla F.,Abou Hachem M.,Lee S.K.,Issakidis-Bourguet E.,Svensson B.,Zeeman S.C.,Santelia D.
Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic alpha-amylase.
J. Biol. Chem.
288
33620-33633
2013
4338
Robert X.,Haser R.,Gottschalk T.E.,Ratajczak F.,Driguez H.,Svensson B.,Aghajari N.
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs.
Structure
11
973-984
2003
4339
Robert X.,Haser R.,Mori H.,Svensson B.,Aghajari N.
Oligosaccharide binding to barley alpha-amylase 1.
J. Biol. Chem.
280
32968-32978
2005
4340
Bozonnet S.,Jensen M.T.,Nielsen M.M.,Aghajari N.,Jensen M.H.,Kramhoeft B.,Willemoes M.,Tranier S.,Haser R.,Svensson B.
The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity.
FEBS J.
274
5055-5067
2007
4341
Nielsen M.M.,Seo E.S.,Bozonnet S.,Aghajari N.,Robert X.,Haser R.,Svensson B.
Multi-site substrate binding and interplay in barley alpha-amylase 1.
FEBS Lett.
582
2567-2571
2008
