| BSSL | bile salt-stimulated lipase |
|---|---|
| CBD | carotid body denervation; closed bladder drainage; common bile duct |
| CBDE | common bile duct exploration |
| CBS | cervicobrachial syndrome; chronic brain syndrome; clinical behavioral science; conjugated bile salts... |
| CD | cadaver donor; canine distemper; canine dose; carbohydrate dehydratase; carbon dioxide; cardiac dise... |
| citrate (pro-3S)-lyase ligase | <enzyme> Deacetylcitrate lyase, acetate and ATP forms citrate lyase, AMP, pi Registry number: EC 6.2.1.22 Synonym: citc gene product, acetate-sh-citrate lyase ligase, citrate lyase ligase (26 Jun 1999) |
|---|---|
| phytanoyl-CoA ligase | <enzyme> An acyl-CoA ligase found in peroxisomes of fibroblasts; it is distinct from palmitoyl-CoA ligase and lignoceroyl-CoA ligase Registry number: EC 6.2.1.- Synonym: phytanoyl-coenzyme a ligase (26 Jun 1999) |
| coronafacate ligase | <enzyme> Required for coronatine biosynthesis by pseudomonas syringae; responsible for the amide linkage of coronafacic acid and coronamic acid; genbank u09027 Registry number: EC 6.3.1.- Synonym: cfl gene product (26 Jun 1999) |
| xenobiotic medium chain fatty acid - coenzyme A ligase | <enzyme> Partial amino acid sequence of enzyme from bovine liver mitochondria given I first source; has high sequence homology to human and rat sa protein Registry number: EC 6.2.1.- Synonym: xl-i ligase, xl-i carboxylic acid - CoA ligase (26 Jun 1999) |
| histidine-trna ligase | <enzyme> An enzyme that activates histidine with its specific transfer RNA. Chemical name: L-Histidine:tRNA(His) ligase (AMP-forming) Registry number: EC 6.1.1.21 (12 Dec 1998) |
| serine-trna ligase | <enzyme> An enzyme that activates serine with its specific transfer RNA. Chemical name: L-Serine:tRNA(Ser) ligase (AMP-forming) Registry number: EC 6.1.1.11 (12 Dec 1998) |
| succinyl-CoA ligase | A ligase reversibly reacting succinate and CoA with ATP to produce ADP, inorganic phosphate, and succinyl-CoA, a similar synthetase, but one able to use itaconate as well as succinate and GTP (or ITP) in place of ATP; a part of the tricarboxylic acid cycle. Synonym: succinic thiokinase, succinyl-CoA ligase. (05 Mar 2000) |
| DNA ligase | <enzyme, molecular biology> Enzyme involved in DNA replication. The DNA ligase of E. Coli seals nicks in one strand of double stranded DNA, a reaction required for linking precursor fragments during discontinuous synthesis on the lagging strand. Nicks are breaks in the phosphodiester linkage that leave a free 3_ OH and 5_ phosphate. The ligase from phage T4 has the additional property of joining two DNA molecules having completely base paired ends. DNA ligases are crucial in joining DNA molecules and preparing radioactive probes (by nick translation) in recombinant DNA technology. (18 Nov 1997) |
| IMP-aspartate ligase | <enzyme> A carbon-nitrogen ligase. During purine ribonucleotide biosynthesis, this enzyme catalyses the synthesis of adenylosuccinate from GTP, imp, and aspartate with the formation of orthophosphate and GDP. Chemical name: IMP:L-aspartate ligase (GDP-forming) Registry number: EC 6.3.4.4 (12 Dec 1998) |
| isoleucine-trna ligase | <enzyme> An enzyme that activates isoleucine with its specific transfer RNA. Chemical name: L-Isoleucine:tRNA(Ile) ligase (AMP-forming) Registry number: EC 6.1.1.5 (12 Dec 1998) |
| threonine-trna ligase | <enzyme> An enzyme that activates threonine with its specific transfer RNA. Chemical name: L-Threonine:tRNA(Thr) ligase (AMP-forming) Registry number: EC 6.1.1.3 (12 Dec 1998) |
| tRNA excision ligase | <enzyme> Processes pre-trna-tyr into mature trna-tyr Registry number: EC 6.5.1.- (26 Jun 1999) |
| tRNA splicing ligase | <enzyme> One of two enzymes involved in trna splicing in archaea Registry number: EC 6.5.1.- (26 Jun 1999) |
| tryptophan-trna ligase | <enzyme> An enzyme that activates tryptophan with its specific transfer RNA. Chemical name: L-Tryptophan:tRNA(Trp) ligase (AMP-forming) Registry number: EC 6.1.1.2 (12 Dec 1998) |
| tubulin-tyrosine ligase | <enzyme> An enzyme that covalently links a tyrosine to the C-terminal glutamyl residue of tubulin, coupled with the hydrolysis of ATP to ADP and Pi; this is a unique posttranslational modification that may have a significant role in cytoskeletal traffic and design. (05 Mar 2000) |