ExplorEnz: Search Results

Your query returned 2 entries. Printable version

1.3.1.101

Accepted name:

2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]

Reaction:

2,3-bis-(O-phytanyl)-sn-glycerol 1-phosphate + 8 NAD(P)⁺ = 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H⁺

For diagram of archaetidylserine biosynthesis, click here

Glossary:

phytanol = (7R,11R,15R)-3,7,11,15-tetramethylhexadecan-1-ol

Other name(s):

digeranylgeranylglycerophospholipid reductase; Ta0516m (gene name); DGGGPL reductase; 2,3-digeranylgeranylglycerophospholipid reductase

Systematic name:

2,3-bis-(O-phytany)l-sn-glycerol 1-phosphate:NAD(P)⁺ oxidoreductase

Comments:

A flavoprotein (FAD). The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids. In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate. cf. EC 1.3.7.11, 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Nishimura, Y. and Eguchi, T. Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum. J. Biochem. 139 (2006) 1073–1081. [DOI] [PMID: 16788058]
2.	Nishimura, Y. and Eguchi, T. Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophilum. Bioorg. Chem. 35 (2007) 276–283. [DOI] [PMID: 17275067]
3.	Xu, Q., Eguchi, T., Mathews, I.I., Rife, C.L., Chiu, H.J., Farr, C.L., Feuerhelm, J., Jaroszewski, L., Klock, H.E., Knuth, M.W., Miller, M.D., Weekes, D., Elsliger, M.A., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids. J. Mol. Biol. 404 (2010) 403–417. [DOI] [PMID: 20869368]

[EC 1.3.1.101 created 2013]

1.21.98.5

Accepted name:

tetraether lipid synthase

Reaction:

(1) 2 a 2,3-bis-O-phytanyl-sn-glycero-phospholipid + 4 S-adenosyl-L-methionine + 2 reduced acceptor = a glycerol dibiphytanyl glycerol tetraether phospholipid + 4 L-methionine + 4 5′-deoxyadenosine + 2 acceptor
(2) a 2,3-bis-O-phytanyl-sn-glycero-phospholipid + 2 S-adenosyl-L-methionine + reduced acceptor = a macrocyclic archaeol phospholipid + 2 L-methionine + 2 5′-deoxyadenosine + acceptor

Glossary:

2,3-bis-O-phytanyl-sn-glycerol = archaeol

Other name(s):

GDGT/MA synthase; GDGT/MAS; tetraether synthase; Tes; Mj0619 (locus name)

Systematic name:

a 2,3-bis-O-phytanyl-sn-glycero-phospholipid:S-adenosyl-L-methionine,acceptor oxidoreductase (cyclyzing)

Comments:

This archaeal enzyme catalyses a C-C bond formation during the biosynthesis of tetraether lipids. The bond is formed between the termini of two lipid tails from two glycerophospholipids to generate the macrocycle glycerol dibiphytanyl glycerol tetraether (GDGT). The enzyme does not distinguish whether the two lipids are connected in antiparallel or parallel geometry, resulting in formation of two forms of the product, which are known as caldarchaeol and isocaldarchaeol, respectively. The enzyme can also form macrocyclic archaeol phospholipids by joining the two lipid tails of a single substrate molecule. Even though the reaction shown here describes phospholipid substrates, the enzyme can also act on glycolipids or lipids that contains mixed types of polar head groups. The enzyme is a radical SAM enzyme that contains 3 [4Fe-4S] clusters and one mononuclear rubredoxin-like iron ion, each found in a separate domain. The enzyme uses the 5′-deoxyadenosyl radical to initiate the reaction, which involves the formation of an intermediate bond between the substrate carbon and a sulfur of one of the [4Fe-4S] clusters. Two radicals are needed per C-C bond formed. The source of the required additional electrons is not known.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Zeng, Z., Chen, H., Yang, H., Chen, Y., Yang, W., Feng, X., Pei, H. and Welander, P.V. Identification of a protein responsible for the synthesis of archaeal membrane-spanning GDGT lipids. Nat. Commun. 13:1545 (2022). [DOI] [PMID: 35318330]
2.	Lloyd, C.T., Iwig, D.F., Wang, B., Cossu, M., Metcalf, W.W., Boal, A.K. and Booker, S.J. Discovery, structure, and mechanism of a tetraether lipid synthase. Nature (2022) . [DOI] [PMID: 35882349]

[EC 1.21.98.5 created 2022]