Amino acids - Revision history

Nicarney at 16:16, 6 November 2008

2008-11-06T16:16:46Z

2008-11-06T16:10:15Z

2008-11-06T15:45:24Z

2008-11-06T15:42:40Z

2008-11-06T15:35:12Z

2008-11-06T15:32:10Z

2008-11-06T15:30:44Z

2008-11-06T15:25:11Z

2008-11-06T15:24:00Z

2008-11-06T15:23:52Z

@@ Line 41: / Line 41: @@
 '''P = proline'''<br>
-Appears to be complete.
+Appears that it can be synthesized from argine, but cannot be synthesized on its own.
 <br>

@@ Line 49: / Line 49: @@
 '''R = arginine'''<br>
-Appears to be complete.
+Can produce from proline, but does not appear to be able to synthesize arginine on its own.
 <br>

@@ Line 37: / Line 37: @@
 '''N = asparagine'''<br>
-Our organism appears to have no enzyme that makes L-aasparagine from L-aspartate (asparaginases). On the RAST spreadsheet, however, RAST calls an "asparagine family protein" in bps from 1139281-1140141.
+Our organism appears to have no enzyme that makes L-aasparagine from L-aspartate (asparaginases). On the RAST spreadsheet, however, RAST calls an "asparagine family protein" in bps from 1139281-1140141 (EC 6.3.5.4).
 <br>

@@ Line 28: / Line 28: @@
 '''K = lysine'''<br>
-Appears to be complete for biosynthesis, very incomplete for degradation<br>
+Appears to be complete.<br>
 '''L = leucine'''<br>

@@ Line 45: / Line 45: @@
 '''Q = glutamine'''<br>
-Appears to be fairly complete when compared with Haloarcula marismortui, with exceptions being a missing NAD synthase (EC 6.3.5.1), and a carbamoyl-phosphate synthetase (EC 6.3.4.16). A glutamyl-tRNA(Gln) amidotransferase subunit (EC 6.3.5.7) appears to be missing, but the RAST spreadsheet calls several glutamyl-tRNA amidotransferase subunits, listing the EC as 6.3.5.-.
+Appears to be fairly complete when compared with Haloarcula marismortui, with exceptions being a missing NAD synthase (EC 6.3.5.1), semialdehyde dehydrogenase (EC1.2.1.16), a 4-aminobutyrate aminotransferase (EC 2.6.1.19), and a carbamoyl-phosphate synthetase (EC 6.3.4.16). A glutamyl-tRNA(Gln) amidotransferase subunit (EC 6.3.5.7) appears to be missing, but the RAST spreadsheet calls several glutamyl-tRNA amidotransferase subunits, listing the EC as 6.3.5.-. Also, an arginine decarboxylase (EC 4.1.1.19) appears to be missing, but the RAST spreadsheet calls an arginine decarboxylase with this EC number.
 <br>

@@ Line 25: / Line 25: @@
 '''I = isoleucine'''<br>
-Appears to be complete<br>
+Appears to be complete.<br>
 '''K = lysine'''<br>

@@ Line 3: / Line 3: @@
 (an alanine-glyoxylate aminotransferase).
 <br>
 '''C = cysteine'''<br>
 <br>
 '''D = aspartic acid'''<br>
 <br>
 '''E = glutamic acid'''<br>
 <br>
 '''F = phenylalanine'''<br>
 <br>
 '''G = glycine'''<br>
 Appears to be missing EC numbers 2.6.1.44 and 1.4.4.2. The RAST spreadsheet calls 2.6.1.44.
 <br>
 '''H = histidine'''<br>
 Appears to be complete.
 <br>
 '''I = isoleucine'''<br>
 <br>
 '''K = lysine'''<br>
 <br>
 '''L = leucine'''<br>
 <br>
 '''M = methionine'''<br>
 <br>
 '''N = asparagine'''<br>
 Our organism appears to have no enzyme that makes L-aasparagine from L-aspartate (asparaginases). On the RAST spreadsheet, however, RAST calls an "asparagine family protein" in bps from 1139281-1140141.
 <br>
 '''P = proline'''<br>
 <br>
 '''Q = glutamine'''<br>
 Appears to be fairly complete when compared with Haloarcula marismortui, with exceptions being a missing NAD synthase (EC 6.3.5.1), a carbamoyl-phosphate synthetase (EC 6.3.4.16).
 <br>
 '''R = arginine'''<br>
 <br>
 '''S = serine'''<br>
 Matches Haloarcula marismortui, except in RAST KEGG diagram, it appears to be missing enzyme 2.7.8.8, which is a CDP-diacylglycerol-serine O-phosphatidyltransferase. However, according to the RAST spreadsheet, there is a CDP-diacylglycerol-serine O-phosphatidyltransferase from bps 1440328-1439621.
 <br>
 '''T = threonine'''<br>
 Appears to be complete.
 <br>
 '''V = valine'''<br>
 <br>
 '''W = tryptophan'''<br>
 <br>
 '''Y = tyrosine'''<br>
 <br>