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In enzymology, a histidine-tRNA ligase (EC 6.1.1.21) is an enzyme that catalyzes the chemical reaction

The 3 substrates of this enzyme are ATP, L-histidine, and tRNA(His), whereas its 3 products are AMP, diphosphate, and L-histidyl-tRNA(His).

This enzyme participates in histidine metabolism and aminoacyl-trna biosynthesis.

Histidine—tRNA ligase belongs to the family of ligase enzymes, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-histidine:tRNAHis ligase (AMP-forming). Other names in common use include histidyl-tRNA synthetase, histidyl-transfer ribonucleate synthetase, and histidine translase.

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In enzymology, a riboflavinase (EC 3.5.99.1) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are riboflavin and H2O, whereas its two products are ribitol and lumichrome.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is riboflavin hydrolase. This enzyme participates in riboflavin metabolism.

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In enzymology, a cyclopropane-fatty-acyl-phospholipid synthase (EC 2.1.1.79) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are S-adenosyl methionine and phospholipid olefinic fatty acid, whereas its two products are S-adenosylhomocysteine and phospholipid cyclopropane fatty acid.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase (cyclizing). Other names in common use include cyclopropane synthetase, unsaturated-phospholipid methyltransferase, cyclopropane synthase, cyclopropane fatty acid synthase, cyclopropane fatty acid synthetase, and CFA synthase.

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1KP9, 1KPG, 1KPH, 1KPI, 1L1E, and 1TPY.

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In enzymology, a 3-hydroxymethylcephem carbamoyltransferase (EC 2.1.3.7) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are carbamoyl phosphate and 3-hydroxymethylceph-3-em-4-carboxylate, whereas its two products are phosphate and 3-carbamoyloxymethylcephem.

This enzyme belongs to the family of transferases, that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases.

The systematic name of this enzyme class is carbamoyl-phosphate:3-hydroxymethylceph-3-em-4-carboxylate carbamoyltransferase.

This enzyme has at least one effector, ATP.

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In enzymology, a lysine carbamoyltransferase (EC 2.1.3.8) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are carbamoyl phosphate and L-lysine, whereas its two products are phosphate and L-homocitrulline.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:L-lysine carbamoyltransferase. This enzyme is also called lysine transcarbamylase.

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In enzymology, a proline—tRNA ligase (EC 6.1.1.15) is an enzyme that catalyzes the chemical reaction

The 3 substrates of this enzyme are ATP, L-proline, and tRNA(Pro), whereas its 3 products are AMP, diphosphate, and L-prolyl-tRNA(Pro).

This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.

This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-proline:tRNAPro ligase (AMP-forming). Other names in common use include prolyl-tRNA synthetase, prolyl-transferRNA synthetase, prolyl-transfer ribonucleate synthetase, proline translase, prolyl-transfer ribonucleic acid synthetase, prolyl-s-RNA synthetase, and prolinyl-tRNA ligase.

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In enzymology, a hexaprenyldihydroxybenzoate methyltransferase (EC 2.1.1.114) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-hexaprenyl-4,5-dihydroxybenzoate, whereas its two products are S-adenosylhomocysteine and 3-hexaprenyl-4-hydroxy-5-methoxybenzoate.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3-hexaprenyl-4,5-dihydroxylate O-methyltransferase. Other names in common use include 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase, and dihydroxyhexaprenylbenzoate methyltransferase. This enzyme participates in ubiquinone biosynthesis.

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Cyclopentadienyl magnesium bromide is a chemical compound with the molecular formula .mw-parser-output .template-chem2-su{display:inline-block;font-size:80%;line-height:1;vertical-align:-0.35em}.mw-parser-output .template-chem2-su>span{display:block;text-align:left}.mw-parser-output sub.template-chem2-sub{font-size:80%;vertical-align:-0.35em}.mw-parser-output sup.template-chem2-sup{font-size:80%;vertical-align:0.65em}C5H5MgBr. The molecule consists of a magnesium atom bonded to a bromine atom and a cyclopentadienyl group, a ring of five carbons each with one hydrogen atom.

The compound is a Grignard reagent, a type of organometallic compound that features a magnesium atom bonded to a halogen atom and to a carbon atom of some organic functional group.

This compound is of historic importance as the starting material for the first published synthesis of ferrocene by Peter Pauson and Thomas J. Kealy in 1951.

The compound can be prepared by reacting cyclopentadiene with magnesium and bromoethane in anhydrous benzene.

MgCpBr

(TiCp2Cl)2
TiCpCl3
TiCp2S5
TiCp2(CO)2
TiCp2Me2

VCpCh
VCp2Cl2
VCp(CO)4

(CrCp(CO)3)2

Fe(i5-C5H4Li)2
((C5H5)Fe(C5H4))2
(C5H4-C5H4)2Fe2
FeCp2PF6
FeCp(CO)2I

CoCp(CO)2

NiCpNO

ZrCp2ClH

MoCp2Cl2
(MoCp(CO)3)2

RuCp(PPh3)2Cl
RuCp(MeCN)3PF6

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In enzymology, a putrescine carbamoyltransferase (EC 2.1.3.6) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are carbamoyl phosphate and putrescine, whereas its two products are phosphate and N-carbamoylputrescine.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:putrescine carbamoyltransferase. Other names in common use include PTCase, putrescine synthase, and putrescine transcarbamylase.

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In enzymology, an oxamate carbamoyltransferase (EC 2.1.3.5) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are carbamoyl phosphate and oxamate, whereas its two products are phosphate and oxalureate.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:oxamate carbamoyltransferase. This enzyme is also called oxamic transcarbamylase. This enzyme participates in purine metabolism.

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