EC 2.7.7

Enzyme that synthesizes DNA from a nucleic acid template

class of enzymes that synthesize RNA from a DNA template

an enzyme which generates DNA from an RNA template, a process termed reverse transcription

thumb|Telomerase catalytic subunit TERT of [[Tribolium castaneum (Red flour beetle), bound to putative RNA template and telomeric DNA (PDB 3KYL)]] thumb|A conceptual diagram showing the protein component of telomerase (TERT) in grey and the RNA component (TR) in yellow

DNA primase is an enzyme involved in the replication of DNA and is a type of RNA polymerase. Primase catalyzes the synthesis of a short RNA (or DNA in some living organisms) segment called a primer complementary to a ssDNA (single-stranded DNA) template. After this elongation, the RNA piece is removed by a 5' to 3' exonuclease and refilled with DNA.

thumb|Ribbon diagram representation of Taq DNA polymerase

DNA-dependent RNA polymerase

enzyme that synthesizes RNA from an RNA template

complex that contains 10 different types of subunits

A transposase is any of a class of enzymes capable of binding to the end of a transposon and catalysing its movement to another part of a genome, typically by a cut-and-paste mechanism or a replicative mechanism, in a process known as transposition. The word "transposase" was coined by the individuals who cloned the enzyme required for transposition of the Tn3 transposon. The existence of transposons was postulated in the late 1940s by Barbara McClintock, who was studying the inheritance of maize, but the actual molecular basis for transposition was described by later groups. McClintock discov

in higher eukaryotes, the polymerase complex that only transcribes ribosomal RNA

family of enzymes

mammalian protein found in Homo sapiens

mammalian protein found in Homo sapiens

enzyme complex

class of enzymes

class of enzymes

InterPro Family

thumb|500x500px|Regulation of bacterial glutamine synthase (GlnA) by adenylylation and (indirectly) by uridylylation. Uridylyltransferase (GlnD) uridylylates the regulatory PII protein (GlnB) which determines whether adenylyltransferase (GlnE) adenylylates or de-adenylylates glutamine synthase. GlnD is a bifunctional enzyme that both attaches and removes UMP from GlnB. GlnD is activated by Alpha-Ketoglutaric acid|α-ketoglutarate and ATP (green) but inhibited by [[glutamine and inorganic phosphate (Pi, in red). The protein names are those in E. coli. Homologs in other bacteria may have differen

class of enzymes

class of enzymes

class of enzymes

class of enzymes

type of enzyme

class of enzymes

family of protein complexes

class of enzymes