Sequence of DHAS_ECOLI
EC Number:1.2.1.11
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
Other sequences found for EC No. 1.2.1.11
General information:
Sequence
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>P0A9Q9|aspartate-semialdehyde dehydrogenase|EC 1.2.1.11|Escherichia coli (strain K12)|Swiss-Prot
MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDL
EALKALDIIVTCQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVIT
DGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMG
HLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSR
EEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNP
WAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLR
RMLRQLA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
152748
Haziza C.,Stragier P.,Patte J.-C.
Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal.
EMBO J.
1
379-384
1982
152749
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
152750
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
152751
Biellmann J.F.,Eid P.,Hirth C.,Jornvall H.
Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties.
Eur. J. Biochem.
104
53-58
1980
152752
Link A.J.,Robison K.,Church G.M.
Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Electrophoresis
18
1259-1313
1997
152753
Karsten W.E.,Viola R.E.
Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli.
Biochim. Biophys. Acta
1121
234-238
1992
152754
Chassagnole C.,Rais B.,Quentin E.,Fell D.A.,Mazat J.P.
An integrated study of threonine-pathway enzyme kinetics in Escherichia coli.
Biochem. J.
356
415-423
2001
152755
Alvarez E.,Ramon F.,Magan C.,Diez E.
L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme.
Biochim. Biophys. Acta
1696
23-29
2004
152756
Hadfield A.,Kryger G.,Ouyang J.,Petsko G.A.,Ringe D.,Viola R.
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J. Mol. Biol.
289
991-1002
1999
152757
Hadfield A.,Shammas C.,Kryger G.,Ringe D.,Petsko G.A.,Ouyang J.,Viola R.E.
Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase.
Biochemistry
40
14475-14483
2001
152758
Nichols C.E.,Dhaliwal B.,Lockyer M.,Hawkins A.R.,Stammers D.K.
High-resolution structures reveal details of domain closure and 'half-of-sites-reactivity' in Escherichia coli aspartate beta-semialdehyde dehydrogenase.
J. Mol. Biol.
341
797-806
2004