|
|
| ID |
Date/Time |
EC/Citation Key |
Table |
Field |
Changed From |
Changed To |
| 601 |
2005-12-08 12:10:17 |
1.14.13.101 |
entry |
class |
|
1 |
| 602 |
2005-12-08 12:10:17 |
1.14.13.101 |
entry |
subclass |
|
14 |
| 603 |
2005-12-08 12:10:17 |
1.14.13.101 |
entry |
subsubclass |
|
13 |
| 604 |
2005-12-08 12:10:17 |
1.14.13.101 |
entry |
serial |
|
101 |
| 606 |
2005-12-08 12:10:18 |
1.14.13.101 |
entry |
diagram |
|
|
| 607 |
2005-12-08 12:10:18 |
1.14.13.101 |
entry |
cas_num |
|
220581-68-0 |
| 617 |
2005-12-08 12:10:18 |
1.14.13.101 |
entry |
glossary |
|
|
| 621 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
ec_num |
|
2.7.4.22 |
| 622 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
common_name |
|
UMP kinase |
| 623 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
reaction |
|
ATP + UMP = ADP + UDP |
| 624 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
other_names |
|
uridylate kinase; UMPK; uridine monophosphate kinase; PyrH; UMP-kinase; SmbA |
| 625 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
sys_name |
|
ATP:UMP phosphotransferase |
| 626 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
comments |
|
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1]. |
| 627 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
links |
|
|
| 628 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
class |
|
2 |
| 629 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
subclass |
|
7 |
| 630 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
subsubclass |
|
4 |
| 631 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
serial |
|
22 |
| 633 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
diagram |
|
|
| 634 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
cas_num |
|
|
| 644 |
2005-12-08 12:25:05 |
2.7.4.22 |
entry |
glossary |
|
|
| 651 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
ec_num |
|
2.4.1.243 |
| 652 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
common_name |
|
6G-fructosyltransferase |
| 653 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
reaction |
|
[1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n ≥ 0) |
| 654 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
other_names |
|
fructan:fructan 6G-fructosyltransferase; 1F(1beta-D-fructofuranosyl)msucrose:1F(1beta-D-fructofuranosyl)nsucrose 6G-fructosyltransferase; 6G-FFT; 6G-FT; 6G-fructotransferase |
| 655 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
sys_name |
|
1F-oligo[ beta-D-fructofuranosyl-(2->1)-]sucrose 6G-beta-D-fructotransferase |
| 656 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
comments |
|
This enzyme catalyses the transfer of the terminal (2->1)-linked beta-D-fructosyl group of a mono- or oligosaccharide substituent on O-1 of the fructose residue of sucrose onto O-6 of its glucose residue [1]. For example, if 1-kestose [1F-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-beta-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see <a href = |
| 657 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
links |
|
|
| 658 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
class |
|
2 |
| 659 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
subclass |
|
4 |
| 660 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
subsubclass |
|
1 |
| 661 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
serial |
|
243 |
| 663 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
diagram |
|
|
| 664 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
cas_num |
|
|
| 674 |
2005-12-09 03:29:51 |
2.4.1.243 |
entry |
glossary |
|
|
| 707 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
ec_num |
|
2.3.1.177 |
| 708 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
common_name |
|
diaminobutyrate acetyltransferase |
| 709 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
reaction |
|
acetyl-CoA + L-2,4-diaminobutanoate = CoA + N-acetyl-L-2,4-diaminobutyrate |
| 710 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
other_names |
|
L-2,4-diaminobutyrate acetyltransferase; L-2,4-diaminobutanoate acetyltransferase; EctA; diaminobutyric acid acetyltransferase; DABA acetyltransferase; 2,4-diaminobutanoate acetyltransferase; DAB acetyltransferase; DABAcT |
| 711 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
sys_name |
|
acetyl-CoA:L-2,4-diaminobutanoate acetyltransferase |
| 712 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
comments |
|
Requires Na+ or K+ for maximal activity [3]. Ornithine, lysine, aspartate, and alpha-, beta- and gamma-aminobutyrate cannot act as substrates [3]. However, acetyl-CoA can be replaced by propanoyl-CoA, although the reaction proceeds more slowly [3]. Forms part of the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.6.1.76, diaminobutyrate—2-oxoglutarate transaminase and EC 4.2.1.108, ectoine synthase. |
| 713 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
links |
|
|
| 714 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
class |
|
2 |
| 715 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
subclass |
|
3 |
| 716 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
subsubclass |
|
1 |
| 717 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
serial |
|
177 |
| 719 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
diagram |
|
|
| 720 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
cas_num |
|
|
| 730 |
2005-12-09 04:01:56 |
2.3.1.177 |
entry |
glossary |
|
|
| 732 |
2005-12-09 04:24:32 |
2.4.1.243 |
entry |
comments |
This enzyme catalyses the transfer of the terminal (2->1)-linked beta-D-fructosyl group of a mono- or oligosaccharide substituent on O-1 of the fructose residue of sucrose onto O-6 of its glucose residue [1]. For example, if 1-kestose [1F-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-beta-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see <a href = |
This enzyme catalyses the transfer of the terminal (2->1)-linked beta-D-fructosyl group of a mono- or oligosaccharide substituent on O-1 of the fructose residue of sucrose onto O-6 of its glucose residue [1]. For example, if 1-kestose [1F-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-beta-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see <a target = "new" href = "http://www.chem.qmul.ac.uk/iupac/2carb/36.html#362">http://www.chem.qmul.ac.uk/iupac/2carb/36.html#362</a>). Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor. Side reactions catalysed are transfer of a beta-D-fructosyl group between compounds of the structure 1F-(1-beta-D-fructofuranosyl)m-6G-(1-beta-D-fructofuranosyl)nsucrose, where m >= 0 and n = 1 for the donor, and m >= 0 and n >= 0 for the acceptor. |
| 760 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
ec_num |
|
4.2.1.108 |
| 761 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
common_name |
|
ectoine synthase |
| 762 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
reaction |
|
N-acetyl-L-2,4-diaminobutyrate = L-ectoine + H2O |
| 763 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
other_names |
|
N-acetyldiaminobutyrate dehydratase; N-acetyldiaminobutanoate dehydratase; L-ectoine synthase; EctC |
| 764 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
sys_name |
|
N-acetyl-L-2,4-diaminobutyrate hydro-lyase |
| 765 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
comments |
|
Ectoine is an osmoprotectant that is found in halophilic eubacteria. This is the third enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.6.1.76, diaminobutyrate—2-oxoglutarate transaminase and EC 2.3.1.177, diaminobutyrate acetyltransferase [1,2]. |
| 766 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
links |
|
|
| 767 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
class |
|
4 |
| 768 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
subclass |
|
2 |
| 769 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
subsubclass |
|
1 |
| 770 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
serial |
|
108 |
| 772 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
diagram |
|
|
| 773 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
cas_num |
|
|
| 783 |
2005-12-09 04:34:12 |
4.2.1.108 |
entry |
glossary |
|
ectoine = 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylate |
| 789 |
2005-12-09 04:48:20 |
1.13.11.19 |
entry |
reaction |
cysteamine + O2 = hypotaurine |
2-aminoethanethiol + O2 = hypotaurine |
| 790 |
2005-12-09 04:48:20 |
1.13.11.19 |
entry |
other_names |
persulfurase; cysteamine oxygenase |
persulfurase; cysteamine oxygenase; cysteamine:oxygen oxidoreductase |
| 791 |
2005-12-09 04:48:20 |
1.13.11.19 |
entry |
sys_name |
cysteamine:oxygen oxidoreductase |
2-aminoethanethiol:oxygen oxidoreductase |
| 792 |
2005-12-09 04:48:20 |
1.13.11.19 |
entry |
comments |
An iron protein. |
A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3]. |
| 800 |
2005-12-09 05:25:21 |
2.3.1.11 |
entry |
reaction |
acetyl-CoA + thioethanolamine = CoA + S-acetylthioethanolamine |
acetyl-CoA + 2-aminoethanethiol = CoA + S-(2-aminoethyl) thioacetate |
| 801 |
2005-12-09 05:25:21 |
2.3.1.11 |
entry |
other_names |
thioltransacetylase B; thioethanolamine acetyltransferase |
thioltransacetylase B; thioethanolamine acetyltransferase; acetyl-CoA:thioethanolamine S-acetyltransferase |
| 802 |
2005-12-09 05:25:21 |
2.3.1.11 |
entry |
sys_name |
acetyl-CoA:thioethanolamine S-acetyltransferase |
acetyl-CoA:2-aminoethanethiol S-acetyltransferase |
| 803 |
2005-12-09 05:25:21 |
2.3.1.11 |
entry |
comments |
|
2-Sulfanylethanol (2-mercaptoethanol) can act as a substrate [1]. |
| 816 |
2005-12-09 05:32:29 |
3.6.3.44 |
entry |
other_names |
multidrug-resistance protein, P-glycoprotein |
multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting) |
| 817 |
2005-12-09 05:32:29 |
3.6.3.44 |
entry |
comments |
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Enzymes of Gram-positive bacteria and eukaryotic cells that export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them transport glutathione conjugates with drugs. Some also show some 'flippase' (Mg2+-ATPase; EC 3.6.3.1) activity. |
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. The enzyme from Gram-positive bacteria and eukaryotic cells export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them transport glutathione—drug conjugates. Some also show some 'flippase' (Mg2+-ATPase; EC 3.6.3.1) activity. |
| 826 |
2005-12-11 09:37:07 |
3.6.3.45 |
entry |
common_name |
steroid-transporting ATPase |
|
| 827 |
2005-12-11 09:37:07 |
3.6.3.45 |
entry |
reaction |
ATP + H2O + steroidin = ADP + phosphate + steroidout |
|
| 828 |
2005-12-11 09:37:07 |
3.6.3.45 |
entry |
sys_name |
ATP phosphohydrolase (steroid-exporting) |
|
| 829 |
2005-12-11 09:37:07 |
3.6.3.45 |
entry |
comments |
ABC-type (ATP-binding cassette-type) ATPase, characterised by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast protein that exports a variety of xenobiotics, especially steroids. |
|
| 830 |
2005-12-11 09:37:07 |
3.6.3.45 |
entry |
links |
BRENDA, ERGO, EXPASY, GO, IUBMB, KEGG |
|
| 838 |
2005-12-11 09:37:07 |
3.6.3.45 |
hist |
note |
|
steroid-transporting ATPase . Now included with EC 3.6.3.44, xenobiotic-transporting ATPase |
| 840 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
ec_num |
|
3.2.1.160 |
| 841 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
common_name |
|
xyloglucan-specific exo-beta-1,4-glucanase |
| 842 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
reaction |
|
xyloglucan + H2O = xyloglucan oligosaccharides (exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan) |
| 843 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
other_names |
|
Cel74A |
| 844 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
sys_name |
|
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucohydrolase |
| 845 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
comments |
|
The enzyme from Chrysosporium lucknowense is an endoglucanase, i.e. acquires the specificity of EC 3.2.1.151, xyloglucan-specific endo-β-1,4-glucanase, when it acts on linear substrates without bulky substituents on the polymeric backbone (e.g. carboxymethylcellulose). However, it switches to an exoglucanase mode of action when bulky side chains are present (as in the case of xyloglucan). The enzyme can also act on barley beta-glucan, but more slowly. |
| 846 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
links |
|
|
| 847 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
class |
|
3 |
| 848 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
subclass |
|
2 |
| 849 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
subsubclass |
|
1 |
| 850 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
serial |
|
160 |
| 852 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
diagram |
|
|
| 853 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
cas_num |
|
|
| 861 |
2005-12-11 09:40:48 |
3.2.1.160 |
hist |
note |
|
|
| 863 |
2005-12-11 09:40:48 |
3.2.1.160 |
entry |
glossary |
|
|
| 865 |
2005-12-11 09:42:42 |
3.2.1.151 |
entry |
other_names |
XEG; xyloglucan endo-beta-1,4-glucanase; xyloglucanase; xyloglucanendohydrolase (XH) |
XEG; xyloglucan endo-beta-1,4-glucanase; xyloglucanase; xyloglucanendohydrolase (XH); 1,4-beta-D-glucan glucanohydrolase |
| 866 |
2005-12-11 09:42:42 |
3.2.1.151 |
entry |
sys_name |
1,4-beta-D-glucan glucanohydrolase |
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucanohydrolase |
| 874 |
2005-12-11 09:48:06 |
2.4.1.195 |
entry |
common_name |
thiohydroximate beta-D-glucosyltransferase |
N-hydroxythioamide S-beta-glucosyltransferase |
| 875 |
2005-12-11 09:48:06 |
2.4.1.195 |
entry |
reaction |
UDP-glucose + phenylthioacetohydroximate = UDP + desulfoglucotropeolin |
UDP-glucose + N-hydroxy-2-phenylethanethioamide = UDP + desulfoglucotropeolin |
| 876 |
2005-12-11 09:48:06 |
2.4.1.195 |
entry |
other_names |
desulfoglucosinolate-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-thiohydroximate glucosyltransferase |
desulfoglucosinolate-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-thiohydroximate glucosyltransferase; thiohydroximate beta-D-glucosyltransferase; UDPG:thiohydroximate glucosyltransferase; thiohydroximate S-glucosyltransferase; thiohydroximate glucosyltransferase; UDP-glucose:thiohydroximate S-β-D-glucosyltransferase |
| 888 |
2005-12-11 09:58:05 |
2.3.1.109 |
entry |
other_names |
arginine succinyltransferase |
arginine succinyltransferase; AstA; arginine and ornithine N2-succinyltransferase; AOST; AST |
| 889 |
2005-12-11 09:58:05 |
2.3.1.109 |
entry |
comments |
Also acts on L-ornithine. |
Also acts on L-ornithine. This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [2,6]. |
| 900 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
ec_num |
|
3.5.3.23 |
| 901 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
common_name |
|
N-succinylarginine dihydrolase |
| 902 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
reaction |
|
N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2 |
| 903 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
other_names |
|
N2-succinylarginine dihydrolase; arginine succinylhydrolase; SADH; AruB; AstB |
| 904 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
sys_name |
|
N2-succinyl-L-arginine iminohydrolase (decarboxylating) |
| 905 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
comments |
|
Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase). |
| 906 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
links |
|
|
| 907 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
class |
|
3 |
| 908 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
subclass |
|
5 |
| 909 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
subsubclass |
|
3 |
| 910 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
serial |
|
23 |
| 912 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
diagram |
|
|
| 913 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
cas_num |
|
|
| 923 |
2005-12-11 10:09:00 |
3.5.3.23 |
entry |
glossary |
|
|
| 926 |
2005-12-11 10:12:40 |
2.6.1.81 |
entry |
ec_num |
|
2.6.1.81 |
| 927 |
2005-12-11 10:12:40 |
2.6.1.81 |
entry |
common_name |
|
succinylornithine transaminase |
| 928 |
2005-12-11 10:12:40 |
2.6.1.81 |
entry |
reaction |
|
N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate |
| 929 |
2005-12-11 10:12:40 |
2.6.1.81 |
entry |
other_names |
|
succinylornithine aminotransferase; N2-succinylornithine 5-aminotransferase; AstC; SOAT |
| 930 |
2005-12-11 10:12:40 |
2.6.1.81 |
entry |
sys_name |
|
N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase |
