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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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cellular amino acid metabolic process
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1 term
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Biochemical function
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catalytic activity
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4 terms
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DOI no:
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Biochemistry
41:11711-11720
(2002)
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PubMed id:
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X-ray structures of threonine aldolase complexes: structural basis of substrate recognition.
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C.L.Kielkopf,
S.K.Burley.
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ABSTRACT
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L-Threonine acetaldehyde-lyase (threonine aldolase, TA) is a
pyridoxal-5'-phosphate-dependent (PLP) enzyme that catalyzes conversion of
L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary
glycine biosynthetic pathway. X-ray structures of Thermatoga maritima TA have
been determined as the apo-enzyme at 1.8 A resolution and bound to substrate
L-allo-threonine and product glycine at 1.9 and 2.0 A resolution, respectively.
Despite low pairwise sequence identities, TA is a member of aspartate
aminotransferase (AATase) fold family of PLP enzymes. The enzyme forms a 222
homotetramer with the PLP cofactor bound via a Schiff-base linkage to Lys199
within a domain interface. The structure reveals bound calcium and chloride ions
that appear to contribute to catalysis and oligomerization, respectively.
Although L-threonine and L-allo-threonine are substrates for T. maritima TA,
enzymatic assays revealed a strong preference for L-allo-threonine. Structures
of the external aldimines with substrate/product reveal a pair of histidines
that may provide flexibility in substrate recognition. Variation in the
threonine binding pocket may explain preferences for L-allo-threonine versus
L-threonine among TA family members.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Dückers,
K.Baer,
S.Simon,
H.Gröger,
and
W.Hummel
(2010).
Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic beta-hydroxy-alpha-amino acids.
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Appl Microbiol Biotechnol, 88,
409-424.
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A.J.Edgar
(2005).
Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene.
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BMC Genomics, 6,
32.
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H.Misono,
H.Maeda,
K.Tuda,
S.Ueshima,
N.Miyazaki,
and
S.Nagata
(2005).
Characterization of an inducible phenylserine aldolase from Pseudomonas putida 24-1.
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Appl Environ Microbiol, 71,
4602-4609.
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Y.K.Kim,
L.Furic,
L.Desgroseillers,
and
L.E.Maquat
(2005).
Mammalian Staufen1 recruits Upf1 to specific mRNA 3'UTRs so as to elicit mRNA decay.
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Cell, 120,
195-208.
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A.Paiardini,
F.Bossa,
and
S.Pascarella
(2004).
Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold-type I, pyridoxal-5'-phosphate-dependent enzymes.
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Protein Sci, 13,
2992-3005.
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B.Cellini,
M.Bertoldi,
A.Paiardini,
S.D'Aguanno,
and
C.B.Voltattorni
(2004).
Site-directed mutagenesis provides insight into racemization and transamination of alanine catalyzed by Treponema denticola cystalysin.
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J Biol Chem, 279,
36898-36905.
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G.Jander,
S.R.Norris,
V.Joshi,
M.Fraga,
A.Rugg,
S.Yu,
L.Li,
and
R.L.Last
(2004).
Application of a high-throughput HPLC-MS/MS assay to Arabidopsis mutant screening; evidence that threonine aldolase plays a role in seed nutritional quality.
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Plant J, 39,
465-475.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
