PMID:795658: Difference between revisions
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!align=left |Citation | |||
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'''Schiltz, E and Schnackerz, KD ''' (1976) Sequence studies on D-serine dehydratase of Escherichia coli. Primary structure of the tryptic phosphopyridoxyl peptide and of the N-terminus. ''Eur. J. Biochem.'' '''71''':109-16 | |||
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!align=left |Abstract | |||
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An improved procedure for large-scale production of crystalline D-serine dehydratase (EC 4.2.1.14) from Escherichia coli is described. The N-terminal sequence of the enzyme (Mr 45500) was determined in a solid-phase sequencer as Met-Glu-Asn-Ala-Lys-Met-Asn-Ser-Leu-Ile-Ala-Gln-Tyr-Pro-Leu-Val-Lys-Asp-Leu-Val-Ala-LEU-Lys. Four of the first five N-terminal residues are homologeous with tryptophanase, another pyridoxal-phosphate (P-Pxy) enzyme that catalyzes alpha,beta-elimination reactions. After borohydride reduction and tryptic digestion of the enzyme, a peptide was isolated showing the sequence Lys-Asp-Ser-His-Leu-Pro-Ile-Ser-Gly-Ser-Ile-Lys(P-Pxy)-Ala-Arg. No clear homology of this portion of the enzyme with tryptophanase or another pyridoxal-phosphate enzyme was observed. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=795658 PubMed] | |||
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!align=left |Keywords | |||
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Amino Acid Sequence; Crystallization; Escherichia coli/enzymology; L-Serine Dehydratase/isolation & purification; Peptide Fragments/analysis; Protein Binding; Pyridoxal Phosphate/analysis; Trypsin | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | |||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
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==See also== | |||
==References== | |||
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Revision as of 06:57, 4 March 2013
| Citation |
Schiltz, E and Schnackerz, KD (1976) Sequence studies on D-serine dehydratase of Escherichia coli. Primary structure of the tryptic phosphopyridoxyl peptide and of the N-terminus. Eur. J. Biochem. 71:109-16 |
|---|---|
| Abstract |
An improved procedure for large-scale production of crystalline D-serine dehydratase (EC 4.2.1.14) from Escherichia coli is described. The N-terminal sequence of the enzyme (Mr 45500) was determined in a solid-phase sequencer as Met-Glu-Asn-Ala-Lys-Met-Asn-Ser-Leu-Ile-Ala-Gln-Tyr-Pro-Leu-Val-Lys-Asp-Leu-Val-Ala-LEU-Lys. Four of the first five N-terminal residues are homologeous with tryptophanase, another pyridoxal-phosphate (P-Pxy) enzyme that catalyzes alpha,beta-elimination reactions. After borohydride reduction and tryptic digestion of the enzyme, a peptide was isolated showing the sequence Lys-Asp-Ser-His-Leu-Pro-Ile-Ser-Gly-Ser-Ile-Lys(P-Pxy)-Ala-Arg. No clear homology of this portion of the enzyme with tryptophanase or another pyridoxal-phosphate enzyme was observed. |
| Links | |
| Keywords |
Amino Acid Sequence; Crystallization; Escherichia coli/enzymology; L-Serine Dehydratase/isolation & purification; Peptide Fragments/analysis; Protein Binding; Pyridoxal Phosphate/analysis; Trypsin |
| edit table |
Significance
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Useful Materials and Methods
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Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
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EcoliWiki Links
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References
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