1w27: Difference between revisions

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==Overview==

Because of its key role in secondary phenylpropanoid metabolism, Phe, ammonia-lyase is one of the most extensively studied plant enzymes. To, provide a basis for detailed structure-function studies, the enzyme from, parsley (Petroselinum crispum) was crystallized, and the structure was, elucidated at 1.7-A resolution. It contains the unusual electrophilic, 4-methylidene-imidazole-5-one group, which is derived from a tripeptide, segment in two autocatalytic dehydration reactions. The enzyme resembles, His ammonia-lyase from the general His degradation pathway but contains, 207 additional residues, mainly in an N-terminal extension rigidifying a, domain interface and in an inserted alpha-helical domain restricting the, access to the active center. Presumably, Phe ammonia-lyase developed from, His ammonia-lyase when fungi and plants diverged from the other kingdoms., A pathway of the catalyzed reaction is proposed in agreement with, established biochemical data. The inactivation of the enzyme by a, nucleophile is described in detail.

Because of its key role in secondary phenylpropanoid metabolism, Phe ammonia-lyase is one of the most extensively studied plant enzymes. To provide a basis for detailed structure-function studies, the enzyme from parsley (Petroselinum crispum) was crystallized, and the structure was elucidated at 1.7-A resolution. It contains the unusual electrophilic 4-methylidene-imidazole-5-one group, which is derived from a tripeptide segment in two autocatalytic dehydration reactions. The enzyme resembles His ammonia-lyase from the general His degradation pathway but contains 207 additional residues, mainly in an N-terminal extension rigidifying a domain interface and in an inserted alpha-helical domain restricting the access to the active center. Presumably, Phe ammonia-lyase developed from His ammonia-lyase when fungi and plants diverged from the other kingdoms. A pathway of the catalyzed reaction is proposed in agreement with established biochemical data. The inactivation of the enzyme by a nucleophile is described in detail.

==About this Structure==

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[[Category: Single protein]]

[[Category: Ritter, H.]]

[[Category: Schulz, G.E.]]

[[Category: Schulz, G E.]]

[[Category: DTT]]

[[Category: lyase]]

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[[Category: phenylpropanoid metabolism]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Because of its key role in secondary phenylpropanoid metabolism, Phe, ammonia-lyase is one of the most extensively studied plant enzymes. To, provide a basis for detailed structure-function studies, the enzyme from, parsley (Petroselinum crispum) was crystallized, and the structure was, elucidated at 1.7-A resolution. It contains the unusual electrophilic, 4-methylidene-imidazole-5-one group, which is derived from a tripeptide, segment in two autocatalytic dehydration reactions. The enzyme resembles, His ammonia-lyase from the general His degradation pathway but contains, 207 additional residues, mainly in an N-terminal extension rigidifying a, domain interface and in an inserted alpha-helical domain restricting the, access to the active center. Presumably, Phe ammonia-lyase developed from, His ammonia-lyase when fungi and plants diverged from the other kingdoms., A pathway of the catalyzed reaction is proposed in agreement with, established biochemical data. The inactivation of the enzyme by a, nucleophile is described in detail.
+Because of its key role in secondary phenylpropanoid metabolism, Phe ammonia-lyase is one of the most extensively studied plant enzymes. To provide a basis for detailed structure-function studies, the enzyme from parsley (Petroselinum crispum) was crystallized, and the structure was elucidated at 1.7-A resolution. It contains the unusual electrophilic 4-methylidene-imidazole-5-one group, which is derived from a tripeptide segment in two autocatalytic dehydration reactions. The enzyme resembles His ammonia-lyase from the general His degradation pathway but contains 207 additional residues, mainly in an N-terminal extension rigidifying a domain interface and in an inserted alpha-helical domain restricting the access to the active center. Presumably, Phe ammonia-lyase developed from His ammonia-lyase when fungi and plants diverged from the other kingdoms. A pathway of the catalyzed reaction is proposed in agreement with established biochemical data. The inactivation of the enzyme by a nucleophile is described in detail.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Ritter, H.]]
-[[Category: Schulz, G.E.]]
+[[Category: Schulz, G E.]]
 [[Category: DTT]]
 [[Category: lyase]]
@@ Line 21: / Line 21: @@
 [[Category: phenylpropanoid metabolism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:18:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:39 2008''