Methylthioribulose 1-phosphate dehydratase

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methylthioribulose 1-phosphate dehydratase
4m6r apip.png
X-ray structure of human methylthioribulose 1-phosphate dehydratase (APIP). PDB entry 4m6r [1]
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EC no. 4.2.1.109
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The enzyme methylthioribulose 1-phosphate dehydratase (EC .2.1.109) catalyzes the chemical reaction

5-(methylsulfanyl)-D)ribulose 1-phosphate 5-(methylthio)-2,3-dioxopentyl phosphate + H2

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 5-methyl-5-thio-D-ribulose-1-phosphate 4-hydro-lyase [5-(methylthio)-2,3-dioxopentyl-phosphate-forming]. Other names in common use include 1-PMT-ribulose dehydratase, and S-methyl-5-thio-D-ribulose-1-phosphate hydro-lyase. This enzyme participates in methionine metabolism.

Related Research Articles

<span class="mw-page-title-main">Serine dehydratase</span>

Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and properties vary among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. SDH catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.

<span class="mw-page-title-main">Transsulfuration pathway</span>

The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine. Two transsulfurylation pathways are known: the forward and the reverse.

<span class="mw-page-title-main">Phosphogluconate dehydrogenase (decarboxylating)</span>

In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction

In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (EC 2.1.1.127) is an enzyme that catalyzes the chemical reaction

Acireductone dioxygenase [iron(II)-requiring] (EC 1.13.11.54) is an enzyme that catalyzes the chemical reaction

Acireductone dioxygenase (Ni2+-requiring) (EC 1.13.11.53) is an enzyme that catalyzes the chemical reaction

In enzymology, a S-methyl-5-thioribose-1-phosphate isomerase is an enzyme that catalyzes the chemical reaction

The enzyme 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) catalyzes the chemical reaction

The enzyme ATP-dependent NAD(P)H-hydrate dehydratase catalyzes the chemical reactions

The enzyme dihydroxy-acid dehydratase (EC 4.2.1.9) catalyzes the chemical reaction

In enzymology, a glycerol dehydratase (EC 4.2.1.30) catalyzes the chemical reaction

The enzyme myo-inosose-2 dehydratase (EC 4.2.1.44) catalyzes the chemical reaction

The enzyme propanediol dehydratase (EC 4.2.1.28) catalyzes the chemical reaction

The enzyme (S)-2-methylmalate dehydratase (EC 4.2.1.34) catalyzes the chemical reaction:

<span class="mw-page-title-main">S-methyl-5'-thioadenosine phosphorylase</span>

In enzymology, a S-methyl-5'-thioadenosine phosphorylase is an enzyme that catalyzes the chemical reaction

In enzymology, a S-methyl-5-thioribose kinase is an enzyme that catalyzes the chemical reaction

Acireductone synthase (EC number 3.1.3.77, E1, E-1 enolase-phosphatase) is an enzyme with systematic name 5-(methylsulfanyl)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing). It catalyses the following reaction:

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (EC 3.1.3.87, HK-MTPenyl-1-P phosphatase, MtnX, YkrX) is an enzyme with systematic name 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction

3-hexulose-6-phosphate synthase is an enzyme with systematic name D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming). This enzyme catalyses the following chemical reaction

2,3-diketo-5-methylthiopentyl-1-phosphate enolase is an enzyme with systematic name 2,3-diketo-5-methylthiopentyl-1-phosphate keto-enol-isomerase. This enzyme catalyses the following chemical reaction

References

  1. ↑ Kang, W; Hong, S. H.; Lee, H. M.; Kim, N. Y.; Lim, Y. C.; Le Le, T. M.; Lim, B; Kim, H. C.; Kim, T. Y.; Ashida, H; Yokota, A; Hah, S. S.; Chun, K. H.; Jung, Y. K.; Yang, J. K. (2014). "Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme". Proceedings of the National Academy of Sciences. 111 (1): E54-61. Bibcode:2014PNAS..111E..54K. doi: 10.1073/pnas.1308768111 . PMC   3890807 . PMID   24367089.


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