[1]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A.,
Ecker J.R.,
Palm C.J.,
Federspiel N.A.,
Kaul S.,
White O.,
Alonso J.,
Altafi H.,
Araujo R.,
Bowman C.L.,
Brooks S.Y.,
Buehler E.,
Chan A.,
Chao Q.,
Chen H.,
Cheuk R.F.,
Chin C.W.,
Chung M.K.,
Conn L., ![]()
Conway A.B.,
Conway A.R.,
Creasy T.H.,
Dewar K.,
Dunn P.,
Etgu P.,
Feldblyum T.V.,
Feng J.-D.,
Fong B.,
Fujii C.Y.,
Gill J.E.,
Goldsmith A.D.,
Haas B.,
Hansen N.F.,
Hughes B.,
Huizar L.,
Hunter J.L.,
Jenkins J.,
Johnson-Hopson C.,
Khan S.,
Khaykin E.,
Kim C.J.,
Koo H.L.,
Kremenetskaia I.,
Kurtz D.B.,
Kwan A.,
Lam B.,
Langin-Hooper S.,
Lee A.,
Lee J.M.,
Lenz C.A.,
Li J.H.,
Li Y.-P.,
Lin X.,
Liu S.X.,
Liu Z.A.,
Luros J.S.,
Maiti R.,
Marziali A.,
Militscher J.,
Miranda M.,
Nguyen M.,
Nierman W.C.,
Osborne B.I.,
Pai G.,
Peterson J.,
Pham P.K.,
Rizzo M.,
Rooney T.,
Rowley D.,
Sakano H.,
Salzberg S.L.,
Schwartz J.R.,
Shinn P.,
Southwick A.M.,
Sun H.,
Tallon L.J.,
Tambunga G.,
Toriumi M.J.,
Town C.D.,
Utterback T.,
Van Aken S.,
Vaysberg M.,
Vysotskaia V.S.,
Walker M.,
Wu D.,
Yu G.,
Fraser C.M.,
Venter J.C.,
Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
|
[2]
|
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/prep.2001.1539; PubMed=11812230 [NCBI, ExPASy, EBI, Israel, Japan]
Paris S.,
Wessel P.M.,
Dumas R.;
"Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana.";
Protein Expr. Purif. 24:105-110(2002).
|
[3]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M.,
Narusaka M.,
Kamiya A.,
Ishida J.,
Satou M.,
Sakurai T.,
Nakajima M.,
Enju A.,
Akiyama K.,
Oono Y.,
Muramatsu M.,
Hayashizaki Y.,
Kawai J.,
Carninci P.,
Itoh M.,
Ishii Y.,
Arakawa T.,
Shibata K.,
Shinagawa A.,
Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
|
[4]
|
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-573.
STRAIN=cv. Columbia;
DOI=10.1007/BF00014439; PubMed=8204822 [NCBI, ExPASy, EBI, Israel, Japan]
Ghislain M.,
Frankard V.,
Vandenbossche D.,
Matthews B.,
Jacobs M.;
"Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana.";
Plant Mol. Biol. 24:835-851(1994).
|
[5]
|
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.M509324200; PubMed=16216875 [NCBI, ExPASy, EBI, Israel, Japan]
Curien G.,
Ravanel S.,
Robert M.,
Dumas R.;
"Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity.";
J. Biol. Chem. 280:41178-41183(2005).
|
|
- CATALYTIC ACTIVITY: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
- ENZYME REGULATION: Inhibition of aspartate kinase activity by threonine and leucine and 3-fold activation by cysteine, isoleucine, valine, serine and alanine at 2.5 mM. Partial inhibition of homoserine dehydrogenase activity by threonine and cysteine (14% of activity remaining at saturation with either amino acid). No synergy between the effectors for both activation or inhibition.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=2.6 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH and 20 mM ATP); | | KM=2.3 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH, 20 mM ATP and a saturating concentration of alanine); | | KM=6.5 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH and 50 mM aspartate); | | KM=0.48 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH, 50 mM aspartate and a saturating concentration of alanine); | | KM=290 µM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (at pH 8.0, in the presence of 150 mM KCl and 200 µM NADPH); | |
- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.
- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
- SUBUNIT: Homo- or heterodimer (Potential).
- SUBCELLULAR LOCATION: Plastid, chloroplast.
- SIMILARITY: In the N-terminal section; belongs to the aspartokinase family.
- SIMILARITY: In the C-terminal section; belongs to the homoserine dehydrogenase family.
- SIMILARITY: Contains 2 ACT domains.
- SEQUENCE CAUTION:
- Sequence=AAF24602.1; Type=Erroneous gene model prediction;
- Sequence=CAA50500.2; Type=Erroneous gene model prediction;
|
ExPASy Home page
YPRC Korea
