scholarly journals The Complete Amino Acid Sequence of the Acyl Carrier Protein of Escherichia coli

1968 ◽  
Vol 243 (24) ◽  
pp. 6420-6431 ◽  
Author(s):  
T C Vanaman ◽  
S J Wakil ◽  
R L Hill
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Complete Amino Acid Sequence

Determination of the Complete Amino Acid Sequence of Recombinant Human γ-Interferon Produced in Escherichia coli

1986 ◽  
Vol 6 (4) ◽  
pp. 331-336 ◽  
Author(s):  
SHOJIRO YAMAZAKI ◽  
TSUNEO SHIMAZU ◽  
SHIGENOBU KIMURA ◽  
HIROHIKO SHIMIZU
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Γ Interferon

scholarly journals 3-Oxoacyl-(acyl-carrier protein) reductase from avocado (Persea americana) fruit mesocarp

1990 ◽  
Vol 271 (3) ◽  
pp. 713-720 ◽  
Author(s):  
P S Sheldon ◽  
R G O Kekwick ◽  
C Sidebottom ◽  
C G Smith ◽  
A R Slabas
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Sequence Data ◽  
Acyl Carrier Protein ◽  
Persea Americana ◽  
Cytochrome F ◽  
Immunogold Electron Microscopy ◽  
Carrier Protein ◽  
Putative Gene

The NADPH-linked 3-oxoacyl-(acyl-carrier protein) (ACP) reductase (EC 1.1.1.100), also known as ‘beta-ketoacyl-ACP reductase’, has been purified from the mesocarp of mature avocado pears (Persea americana). The enzyme is inactivated by low ionic strength and low temperature. On SDS/PAGE under reducing conditions, purified 3-oxoacyl-ACP reductase migrated as a single polypeptide giving a molecular mass of 28 kDa. Gel-filtration chromatography gave an apparent native molecular mass of 130 kDa, suggesting that the enzyme is tetrameric. The enzyme is inactivated by dilution, but some protection is afforded by the presence of NADPH. Kinetic constants have been determined using synthetic analogues as well as the natural ACP substrate. It exhibits a broad pH optimum around neutrality. Phenylglyoxal inactivates the enzyme, and partial protection is given by 1 mM-NADPH. Antibodies have been raised against the protein, which were used to localize it using immunogold electron microscopy. It is localized in plastids. N-Terminal amino-acid-sequence analysis was performed on the enzyme, and it shows close structural similarity with cytochrome f. Internal amino-acid-sequence data, derived from tryptic peptides, shows similarity with the putative gene products encoded by the nodG gene from the nitrogen-fixing bacterium Rhizobium meliloti and the gra III act III genes from Streptomyces spp.

scholarly journals The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product

1986 ◽  
Vol 237 (2) ◽  
pp. 427-437 ◽  
Author(s):  
G Millar ◽  
A Lewendon ◽  
M G Hunter ◽  
J R Coggins
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Transcriptional Start Site ◽  
Cloning And Expression ◽  
Potential Operator ◽  
Gene Encoding ◽  
Shikimate Kinase ◽  
Complete Amino Acid Sequence ◽  
Escherichia Coli K12

The aroL gene encoding the enzyme shikimate kinase II was cloned from Escherichia coli K12. Construction of over-expressing strains permitted for the first time the purification to homogeneity of a monofunctional shikimate kinase. The complete amino acid sequence of shikimate kinase II was determined by a combined nucleotide and direct amino acid sequencing strategy. E. coli shikimate kinase II is a monomeric enzyme containing 173 amino acid residues with a calculated Mr 18,937. The amino acid sequence contains a region homologous with other kinases and ATP-requiring enzymes. Evidence is presented suggesting that the transcriptional start site of the aroL gene is located within a potential operator site.

scholarly journals The Complete Amino-Acid Sequence of Elongation Factor Tu from Escherichia coli

1980 ◽  
Vol 108 (2) ◽  
pp. 507-526 ◽  
Author(s):  
Michael D. JONES ◽  
Karen M. NIELSEN ◽  
Brian F. C. CLARK ◽  
Torben E. PETERSEN ◽  
Staffan MAGNUSSON ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Elongation Factor ◽  
Elongation Factor Tu ◽  
Complete Amino Acid Sequence
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