Abstract：
:Sucrose-phosphate synthase (SPS; EC 2.4.1.14) is regulated in part by reversible protein phosphorylation. When dephospho-SPS is partially purified from illuminated spinach leaves and incubated with [gamma-32P]ATP the enzyme is phosphorylated by a copurifying protein kinase. In this report, 32P-phosphopeptides from tryptic digests of in vitro phosphorylated SPS were purified by metal-ion affinity chromatography and reversed-phase high-performance liquid chromatography. Three distinct 32P-phosphopeptides were resolved. Edman sequencing of the major phosphopeptide (which contained > 80% of the total 32P) identified the amino acid sequence as Ile-Ser-Ser(P)-Val-Glu-Met-Met-Asp-Asn-Trp-Ala-Asn-Thr-Phe-Lys. This sequence corresponds to residues 156 to 170 of the deduced amino acid sequence of spinach SPS [Klein, R. R., Crafts-Brandner, S. J., and Salvucci, M. E. (1993) Planta 190, 498-510, and Sonnewald, U., Quick, W. P., MacRae, E., Krause, K.-P., and Stitt, M. (1993) Planta 189, 174-181]. Identification of the phosphoseryl residue was accomplished by manual Edman sequencing. The two other phosphopeptides, which each contained less than 10% of the total 32P, were not sequenced. An Escherichia coli expressed, 26-kDa fragment of SPS which contains the major phosphorylation site was a substrate for the protein kinase which copurifies with SPS. Two-dimensional peptide mapping analysis of this fragment showed the major phosphopeptide was present but not the other site(s), suggesting that other peptides are derived from a site other than Ser158. These results provide additional indirect evidence for the presence of multiple phosphorylation sites in SPS.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
McMichael RW Jr,Klein RR,Salvucci ME,Huber SCdoi
10.1006/abbi.1993.1586subject
Has Abstractpub_date
1993-12-01 00:00:00pages
248-52issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(83)71586-9journal_volume
307pub_type
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更新日期：1995-05-10 00:00:00
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doi：10.1006/abbi.1995.1122
更新日期：1995-02-01 00:00:00
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doi：10.1006/abbi.1998.0849
更新日期：1998-10-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1006/abbi.1994.1079
更新日期：1994-02-15 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章,评审
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更新日期：1990-12-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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更新日期：2004-08-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1016/0003-9861(83)90247-3
更新日期：1983-07-15 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1016/0003-9861(90)90483-f
更新日期：1990-06-01 00:00:00
abstract：:Liver mitochondria provided with an oxidizable substrate, ATP, oxygen, and an ADP-generating system (soluble F1-ATPase) were used to reevaluate the rate-controlling step(s) intrinsic to all of the processes of mitochondrial oxidative phosphorylation. The quantity termed "control strength" (C), previously defined as th...
journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1016/0003-9861(84)90481-8
更新日期：1984-09-01 00:00:00
