 |
PDBsum entry 1jf5
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Role of phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by thermoactinomyces vulgaris r-47 alpha-Amylase 2 (tvaii). X-Ray structures of the mutant tvaiis, F286a and f286y, And kinetic analyses of the phe286-Replaced mutant tvaiis.
|
|
|
Authors
|
|
A.Ohtaki,
S.Kondo,
Y.Shimura,
T.Tonozuka,
Y.Sakano,
S.Kamitori.
|
|
|
Ref.
|
|
Carbohydr Res, 2001,
334,
309-313.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Phe286 located in the center of the active site of alpha-amylase 2 from
Thermoactinomyces vulgaris R-47 (TVAII) plays an important role in the substrate
recognition for cyclomaltooligosaccharides (cyclodextrins). The X-ray structures
of mutant TVAIIs with the replacement of Phe286 by Ala (F286A) and Tyr (F286Y)
were determined at 3.2 A resolution. Their structures have no significant
differences from that of the wild-type enzyme. The kinetic analyses of
Phe286-replaced variants showed that the variants with non-aromatic residues,
Ala (F286A) and Leu (F286L), have lower enzymatic activities than those with
aromatic residues, Tyr (F286Y) and Trp (F286W), and the replacement of Phe286
affects enzymatic activities for CDs more than those for starch.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystal structure of thermoactinomyces vulgaris r-47 alpha-Amylase ii (tvaii) hydrolyzing cyclodextrins and pullulan at 2.6 a resolution.
|
|
|
Authors
|
|
S.Kamitori,
S.Kondo,
K.Okuyama,
T.Yokota,
Y.Shimura,
T.Tonozuka,
Y.Sakano.
|
|
|
Ref.
|
|
J Mol Biol, 1999,
287,
907-921.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 7.
Figure 7. Stereoviews of the active site structures of (a) TVAII and (b) CGT8. Superimposed b-CD moieties are
shown by broken lines in (a), and a binding b-CD moiety is shown by thin lines in (b).
|
|
Figure 8.
Figure 8. Stereoview of the dimer structure of TVAII viewed from the non-crystallographic 2-fold axis as illustrated
by the program MOLSCRIPT. Mol-2 is shown in the light colors.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from Elsevier
|
|
|
|
|
|
|
